{% extends "layout.html" %}
{% block extraheaders %}
{% endblock extraheaders %}
{% block title %}
CNCD
{% endblock title %}
{% block body %}
High voltage device controller.
This is a wider card with supporting text below as a natural lead-in to additional content. This content is a little bit longer.
Webcam {{ camera.name }}.
Open Stream {{ handle }}{{ action.command }} - {{ action.long }} - {{ action.short }}
{% endfor %} {% endblock body %}


| Left |
Result |
|
Right |
| 1 | char | |
| char | | as is |
| literal2 | | high-order 8 bits discarded |
| literal4 | | high 3 bytes discarded |
|
| 2 | literal2 | |
| char | | high-order 8 bits are 0 |
| literal2 | | as is |
| literal4 | | high 2 bytes discarded |
|
| 3 | integers | |
char,literal2 or literal4 |
| 4 | literal2 | |
integers in the range -65536 to 65535 |
| 5 | char | |
literal2 or literal4 in the range 0 to 255 |
| 6 | literal2 | |
pairs of chars are converted to literal2s |
| 7 | char or U16 | |
| U8 | | converted to U16 |
| ASCII | | as is |
| literal2 | | if all values <128, convert to ASCII, otherwise as is |
| U32 | | if all values <128, convert to ASCII, otherwise converted to U16 |
| integers | | the range 0 to 16b10ffff converted to U16 |
an empty right argument produces an empty char result
|
| 8 | U8 | |
| U16 | | converted to U8 |
| U32 | | converted to U8 |
| char | | as is |
| integers | | the range 0 to 16b10ffff converted to U8 |
an empty right argument produces an empty char result
|
| 9 | char or U32 | |
| U8 | | converted to U32 |
| ASCII | | as is |
| U16 | | if all values <128, convert to ASCII, otherwise converted to U32 |
| literal4 | | as is, and any valid surrogate pairs are converted |
| integers | | converted to literal4 |
an empty right argument produces an empty char result
|
| 10 | literal4 | |
| char | | promoted to literal4 |
| literal2 | | promoted to literal4 |
| literal4 | | as is |
| integers | | converted to literal4 |
each char or literal2 is promoted to literal4 character by character, no U8 or U16 encoding assumed
|


include "head.html"
include "header.html"
include "fusion-training.html"
include "footer.html" include "foot.html"


Publications |
|
Whiting, M.E., J. Cagan and P. R. LeDuc,
Efficient Probabilistic Grammar Induction for Design.
AI EDAM, Vol 32, No. 2, pp. 177-188, 2018. DOI:
10.1017/S0890060417000464
|
|
Snehalkumar "Neil" S. Gaikwad, Nalin Chhibber, Vibhor Sehgal, Alipta
Ballav, Catherine Mullings, Ahmed Nasser, Angela Richmond-Fuller,
Aaron Gilbee, Dilrukshi Gamage, Mark E. Whiting,
Sharon Zhou, Sekandar Matin, Senadhipathige Niranga, Shirish Goyal,
Dinesh Majeti, Preethi Srinivas, Adam Ginzberg, Kamila Mananova,
Karolina Ziulkoski, Jeff Regino, Tejas Sarma, Akshansh Sinha,
Abhratanu Paul, Christopher Diemert, Mahesh Murag, William Dai,
Manoj Pandey, Rajan Vaish, Michael Bernstein.
Prototype Tasks: Improving Crowdsourcing Results through Rapid,
Iterative Task Design. Fifth AAAI Conference on Human Computation and Crowdsourcing.
2017
HCOMP'17.
|
|
Mark E. Whiting, Dilrukshi Gamage, Shirish Goyal,
Aaron Gilbee, Dinesh Majeti, Angela Richmond-Fuller, Mohamed Hashim
Salih, Tejas Seshadri Sarma, Vinayak Mathur, Manoj Pandey,
Snehalkumar (Neil) S. Gaikwad, Rajan Vaish and Michael S. Bernstein.
Designing A Constitution for a Self-Governing Crowdsourcing
Marketplace. 2017.
CI'17: Collective Intelligence.
|
|
Dilrukshi Gamage, Mark E. Whiting, Thejan
Rajapakshe, Haritha Thilakarathne, Indika Perera, and Shantha
Fernando. 2017.
Improving Assessment on MOOCs Through Peer Identification and
Aligned Incentives. In Proceedings of the Fourth ACM conference on Learning@Scale
L@S'17. ACM, New York, NY, USA. DOI:
10.1145/3051457.3054013
|
|
Mark E. Whiting, Dilrukshi Gamage, Snehalkumar
(Neil) S. Gaikwad, Aaron Gilbee, Shirish Goyal, Alipta Ballav,
Dinesh Majeti, Nalin Chhibber, Angela Richmond-Fuller, Freddie
Vargus, Tejas Seshadri Sarma, Varshine Chandrakanthan, Teogenes
Moura, Mohamed Hashim Salih, Gabriel Bayomi Tinoco Kalejaiye, Adam
Ginzberg, Catherine A. Mullings, Yoni Dayan, Kristy Milland,
Henrique Orefice, Jeff Regino, Sayna Parsi, Kunz Mainali, Vibhor
Sehgal, Sekandar Matin, Akshansh Sinha, Rajan Vaish, and Michael S.
Bernstein. 2017.
Crowd Guilds: Worker-led Reputation and Feedback on
Crowdsourcing Platforms. In Proceedings of the 2017 ACM Conference on Computer Supported
Cooperative Work and Social Computing
CSCW'17. ACM, New
York, NY, USA, 1902-1913. DOI:
10.1145/2998181.2998234
|
|
Snehalkumar (Neil) S. Gaikwad, Mark E. Whiting,
Dilrukshi Gamage, Catherine A. Mullings, Dinesh Majeti, Shirish
Goyal, Aaron Gilbee, Nalin Chhibber, Adam Ginzberg, Angela
Richmond-Fuller, Sekandar Matin, Vibhor Sehgal, Tejas Seshadri
Sarma, Ahmed Nasser, Alipta Ballav, Jeff Regino, Sharon Zhou, Kamila
Mananova, Preethi Srinivas, Karolina Ziulkoski, Dinesh Dhakal,
Alexander Stolzoff, Senadhipathige S. Niranga, Mohamed Hashim Salih,
Akshansh Sinha, Rajan Vaish, and Michael S. Bernstein. 2017.
The Daemo Crowdsourcing Marketplace. In Companion of the 2017 ACM Conference on Computer Supported
Cooperative Work and Social Computing (CSCW'17
Companion). ACM, New York, NY, USA, 1-4. DOI:
10.1145/3022198.3023270
|
|
Whiting, Mark E., Cagan, J. and LeDuc, P., 2017.
Automated Induction of General Grammars for Design. In Design Computing and Cognition'16.
DCC'16
Springer, Cham. 267-278 DOI:
10.1007/978-3-319-44989-0_15
|
|
Snehalkumar (Neil) S. Gaikwad, Durim Morina, Adam Ginzberg,
Catherine Mullings, Shirish Goyal, Dilrukshi Gamage, Christopher
Diemert, Mathias Burton, Sharon Zhou,
Mark E. Whiting, Karolina Ziulkoski, Alipta Ballav,
Aaron Gilbee, Senadhipathige S. Niranga, Vibhor Sehgal, Jasmine Lin,
Leonardy Kristianto, Angela Richmond-Fuller, Jeff Regino, Nalin
Chhibber, Dinesh Majeti, Sachin Sharma, Kamila Mananova, Dinesh
Dhakal, William Dai, Victoria Purynova, Samarth Sandeep, Varshine
Chandrakanthan, Tejas Sarma, Sekandar Matin, Ahmed Nasser, Rohit
Nistala, Alexander Stolzoff, Kristy Milland, Vinayak Mathur, Rajan
Vaish, and Michael S. Bernstein. 2016.
Boomerang: Rebounding the Consequences of Reputation Feedback
on Crowdsourcing Platforms. In Proceedings of the 29th Annual Symposium on User Interface
Software and Technology
UIST'16. ACM,
New York, NY, USA, 625-637. DOI:
10.1145/2984511.2984542
|
|
Lee, J.H., Park, H.J, Lim, S., Kim, S.J., Jung, H. &
Whiting, Mark E., 2010.
A Formal Approach for the Interpretation of Cultural Content:
Evolution of a Korean traditional pattern, Bosangwhamun. Proceedings of Computer Aided Architectural Design in Asia
CAADRIA'10, Hong-Kong Mar.
|
|
Whiting, Mark E. & Varadarajan, S., 2009.
Early Exploration of Cloud Computing for Design Practice &
Education. Proceedings of International Association of Societies of Design
Research IASDR'09,
Seoul Nov.
|


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Mike Croucher’s mystery curve in pure JavaScript. On a device with a keyboard, try selecting one of the sliders and holding down a cursor key to see the patterns evolve continuously.
Complete code for this example:
Examples Page


Gecode::Float::Linear Namespace Reference
Linear propagators More...
Classes | |
| class | TermLess |
| Sort linear terms by view. More... | |
| class | Lin |
| Base-class for n-ary linear propagators. More... | |
| class | Eq |
| Propagator for bounds consistent n-ary linear equality More... | |
| class | Lq |
| Propagator for bounds consistent n-ary linear less or equal More... | |
| class | Term |
| Class for describing linear term . More... | |
Functions | |
| template<class View > | |
| void | eliminate_p (ModEventDelta med, ViewArray< View > &x, FloatVal &c) |
| template<class View > | |
| void | eliminate_n (ModEventDelta med, ViewArray< View > &y, FloatVal &c) |
| bool | infty (const FloatNum &n) |
| void | estimate (Term *t, int n, FloatVal c, FloatNum &l, FloatNum &u) |
| Estimate lower and upper bounds. | |
| FloatView | extend (Home home, Region &r, Term *&t, int &n) |
| Extend terms by adding view for result. | |
| template<class View > | |
| void | post_nary (Home home, ViewArray< View > &x, ViewArray< View > &y, FloatRelType frt, FloatVal c) |
| Posting n-ary propagators. | |
| void | dopost (Home home, Term *t, int n, FloatRelType frt, FloatVal c) |
| void | post (Home home, Term *t, int n, FloatRelType frt, FloatVal c) |
| Post propagator for linear constraint over floats. | |
| void | post (Home home, Term *t, int n, FloatRelType frt, FloatVal c, Reify r) |
| Post propagator for reified linear constraint over floats. |
Detailed Description
Linear propagators
Function Documentation
template<class View >
| void Gecode::Float::Linear::eliminate_p | ( | ModEventDelta | med, | |
| ViewArray< View > & | x, | |||
| FloatVal & | c | |||
| ) | [inline] |
template<class View >
| void Gecode::Float::Linear::eliminate_n | ( | ModEventDelta | med, | |
| ViewArray< View > & | y, | |||
| FloatVal & | c | |||
| ) | [inline] |
| bool Gecode::Float::Linear::infty | ( | const FloatNum & | n | ) | [inline] |
| void Gecode::Float::Linear::estimate | ( | Term * | t, | |
| int | n, | |||
| FloatVal | c, | |||
| FloatNum & | l, | |||
| FloatNum & | u | |||
| ) |
Estimate lower and upper bounds.
Estimates the boundaries for a linear expression . If the boundaries exceed the limits as defined in Limits::Float, these boundaries are returned.
- Parameters:
-
t array of linear terms n size of array c constant l lower bound u upper bound
| FloatView Gecode::Float::Linear::extend | ( | Home | home, | |
| Region & | r, | |||
| Term *& | t, | |||
| int & | n | |||
| ) |
template<class View >
| void Gecode::Float::Linear::post_nary | ( | Home | home, | |
| ViewArray< View > & | x, | |||
| ViewArray< View > & | y, | |||
| FloatRelType | frt, | |||
| FloatVal | c | |||
| ) | [inline] |


Uploading records
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For this question, refer back to the code in linkedchain.java If the first line of the add method was changed from:
Node newNode = new Node(newEntry);
to
Node newNode = new Node(newEntry, null);
hint 2 would go here


---
title: copenhagen penthouse interior by norm architects
date: '2009-05-10T01:24:00+05:30'
tags:
- design
tumblr_url: https://sureshshanmugam.com/post/105546498/copenhagen-penthouse-interior-by-norm-architects
---
Copenhagen Penthouse Interior by Norm Architects » CONTEMPORIST


--- layout: default --- {% assign current_version = page.version %}
You are viewing installation instructions for {{ current_version }}.
Careful!
You are viewing installation instructions for a version of {{ site.title }} that is not the latest release.
Go here to view installation instructions for the latest version.
Looking for even older versions? Learn more.


[gecode-users] question about posting of linear expressions
Guido Tack
tack at gecode.org
Fri Jul 9 09:56:46 CEST 2010
Kish Shen wrote:
> Guido Tack wrote:
>
>>> reif = solver->vBool[b];
>>> ...
>>> reif = post(*solver, c);
>>> ...
>
> Hi Guido,
>
> Thanks for pointing this out. After some trial and error, I think I have now know how to work around the problem. The issue appears to be reif is
> on the left hand side of =, and should be a new (uninitialised) BoolVar - not an existing initialised BoolVar like what I was doing.
Yes, post returns a fresh BoolVar, and the assignment overwrites the previous variable (so it usually only makes sense if it's uninitialized).
> After the assignment, reif can then be linked to an existing BoolVar like solver->vBool[b], or an integer value (0 or 1).
Right. But any linking has to be done by constraints (such as eqv), never by C++ assignment. In your case, I'd try to reuse the existing BoolVars as much as possible, only creating new variables if it cannot be avoided. In general, using
post(*solver, tt(eqv(c,b)));
will be more efficient than
BoolVar reif = post(*solver, c);
post(*solver, eqv(reif,b));
If the distinction is just between variable or 0/1 constant, you could simply add two assigned BoolVars to the array (one for 0 and one for 1), so that the posting becomes more uniform. The post function analyzes the arguments anyway and will post the most efficient propagators (e.g. it won't post reified propagators if the reification is statically 1 or 0).
Cheers,
Guido
--
Guido Tack, http://people.cs.kuleuven.be/~guido.tack/
More information about the users
mailing list


%perl> my $username = undef; $username = $Mech->{sess}->param('member') unless $Mech->{sess}->is_empty(); if (defined $username && length $username) { $m->comp('/site/sitehandler.mas:logout'); } print qq{
You should now be redirected to the main page.
}; $r->header_out('Refresh' => '0; url="/"'); %perl> <%method is_logout> # this does nothing, it's here to tell autohandler not to say 'expired' # if the user is in the process of logging out. %method> <%method is_public> # this does nothing, it's here to tell autohandler that we can be called # even when we're not logged in. %method> <%method tg_not_needed> # tells sitehandler.mas:request_ok that we don't need a trustgroup here %method> <%method vetting_not_needed> # tells sitehandler.mas:request_ok that we don't need vetting here %method>


We aggregate tables!
- utilize plug-and-play content
- generate bricks-and-clicks partnerships
- unleash cutting-edge vortals
- synthesize cutting-edge partnerships
- aggregate one-to-one bandwidth
- innovate leading-edge metrics
- benchmark rich e-markets
- evolve transparent architectures
- leverage value-added experiences
- benchmark scalable initiatives


setlocale
, localeconv
—select or query locale#include <locale.h> char *setlocale(int category, const char *locale); lconv *localeconv(void); char *_setlocale_r(void *reent, int category, const char *locale); lconv *_localeconv_r(void *reent);
Description
setlocale
is the facility defined by ANSI C to condition the
execution environment for international collating and formatting
information; localeconv
reports on the settings of the current
locale.
This is a minimal implementation, supporting only the required "POSIX"
and "C"
values for locale; strings representing other locales are not
honored unless _MB_CAPABLE is defined.
If _MB_CAPABLE is defined, POSIX locale strings are allowed, following the form
language[_TERRITORY][.charset][@modifier]
"language"
is a two character string per ISO 639, or, if not available
for a given language, a three character string per ISO 639-3.
"TERRITORY"
is a country code per ISO 3166. For "charset"
and
"modifier"
see below.
Additionally to the POSIX specifier, the following extension is supported
for backward compatibility with older implementations using newlib:
"C-charset"
.
Instead of "C-"
, you can also specify "C."
. Both variations allow
to specify language neutral locales while using other charsets than ASCII,
for instance "C.UTF-8"
, which keeps all settings as in the C locale,
but uses the UTF-8 charset.
The following charsets are recognized:
"UTF-8"
, "JIS"
, "EUCJP"
, "SJIS"
, "KOI8-R"
, "KOI8-U"
,
"GEORGIAN-PS"
, "PT154"
, "TIS-620"
, "ISO-8859-x"
with
1 <= x <= 16, or "CPxxx"
with xxx in [437, 720, 737, 775, 850, 852, 855,
857, 858, 862, 866, 874, 932, 1125, 1250, 1251, 1252, 1253, 1254, 1255, 1256,
1257, 1258].
Charsets are case insensitive. For instance, "EUCJP"
and "eucJP"
are equivalent. Charset names with dashes can also be written without
dashes, as in "UTF8"
, "iso88591"
or "koi8r"
. "EUCJP"
and
"EUCKR"
are also recognized with dash, "EUC-JP"
and "EUC-KR"
.
Full support for all of the above charsets requires that newlib has been
build with multibyte support and support for all ISO and Windows Codepage.
Otherwise all singlebyte charsets are simply mapped to ASCII. Right now,
only newlib for Cygwin is built with full charset support by default.
Under Cygwin, this implementation additionally supports the charsets
"GBK"
, "GB2312"
, "eucCN"
, "eucKR"
, and "Big5"
. Cygwin
does not support "JIS"
.
Cygwin additionally supports locales from the file /usr/share/locale/locale.alias.
(""
is also accepted; if given, the settings are read from the
corresponding LC_* environment variables and $LANG according to POSIX rules.)
This implementation also supports the modifiers "cjknarrow"
and
"cjkwide"
, which affect how the functions wcwidth
and wcswidth
handle characters from the "CJK Ambiguous Width" category of characters
described at http://www.unicode.org/reports/tr11/#Ambiguous.
These characters have a width of 1 for singlebyte charsets and a width of 2
for multibyte charsets other than UTF-8.
For UTF-8, their width depends on the language specifier:
it is 2 for "zh"
(Chinese), "ja"
(Japanese), and "ko"
(Korean),
and 1 for everything else. Specifying "cjknarrow"
or "cjkwide"
forces a width of 1 or 2, respectively, independent of charset and language.
If you use NULL
as the locale argument, setlocale
returns a
pointer to the string representing the current locale. The acceptable
values for category are defined in `locale.h
' as macros
beginning with "LC_"
.
localeconv
returns a pointer to a structure (also defined in
`locale.h
') describing the locale-specific conventions currently
in effect.
_localeconv_r
and _setlocale_r
are reentrant versions of
localeconv
and setlocale
respectively. The extra argument
reent is a pointer to a reentrancy structure.
Returns
setlocale
returns a pointer to a string
associated with the specified category for the new locale. The string
returned by setlocale
is such that a subsequent call using that
string will restore that category (or all categories in case of LC_ALL),
to that state. The application shall not modify the string returned
which may be overwritten by a subsequent call to setlocale
.
On error, setlocale
returns NULL
.
localeconv
returns a pointer to a structure of type lconv
,
which describes the formatting and collating conventions in effect (in
this implementation, always those of the C locale).
Portability
setlocale
, but the only locale required across all
implementations is the C locale.
Notes
No supporting OS subroutines are required.


|
||||||||||
| PREV CLASS NEXT CLASS | FRAMES NO FRAMES | |||||||||
| SUMMARY: NESTED | ENUM CONSTANTS | FIELD | METHOD | DETAIL: ENUM CONSTANTS | FIELD | METHOD |
java.lang.Object java.lang.Enum<Expression.ExpressionType> com.habelitz.jsobjectizer.jsom.api.expression.Expression.ExpressionType
public static enum Expression.ExpressionType
Defines constants for all Expression
suptypes.
| Enum Constant Summary | |
|---|---|
ARRAY_ELEMENT_ACCESS
Constant for static array element accesses, i.e. something like 'AnyArray[offset]' . |
|
ARRAY_TYPE_DECLARATOR
Constant for array type declarators, i.e. something like
'AnyArray[]' . |
|
BINARY_OPERATOR_EXPRESSION
Constant for all expressions with one operator and two operands. |
|
CLASS_CONSTRUCTOR_CALL
Constant for new expressions in the form of class constructor calls, i.e. something like 'new AnyType(constructorArgs) . |
|
CONDITIONAL_EXPRESSION
Constant for conditional expressions. |
|
DOT_EXPRESSION
Constant for DotExpression expression types, i.e. dot
separated primary expressions |
|
EXPLICIT_CONSTRUCTOR_CALL
Constant for explicit this or super
constructor call expressions. |
|
IDENTIFIER
Constant for identifier expressions. |
|
INSTANCEOF_EXPRESSION
Constant for instanceof expressions. |
|
KEYWORD
Constant for the primary expression keywords that are not handled by anything else; these are the keywords class , this
, super and void . |
|
LITERAL
Constant for all kinds of literals. |
|
METHOD_CALL
Constant for method call expressions, i.e. method invocations. |
|
PARENTHESIZED_EXPRESSION
Constant for parenthesized expressions, i.e. expressions enclosed within parentheses. |
|
STATIC_ARRAY_CREATOR
Constant for new expressions in the form of static array creators, i.e. something like 'new AnyType[expression]' or
'new AnyType[] {anyInitializers}' . |
|
TYPE_CAST
Constant for type cast expressions. |
|
UNARY_OPERATOR_EXPRESSION
Constant for all expressions with one operator and one operands. |
| Method Summary | |
|---|---|
static Expression.ExpressionType |
valueOf(java.lang.String name)
Returns the enum constant of this type with the specified name. |
static Expression.ExpressionType[] |
values()
Returns an array containing the constants of this enum type, in the order they are declared. |
| Methods inherited from class java.lang.Enum |
|---|
clone, compareTo, equals, finalize, getDeclaringClass, hashCode, name, ordinal, toString, valueOf |
| Methods inherited from class java.lang.Object |
|---|
getClass, notify, notifyAll, wait, wait, wait |
| Enum Constant Detail |
|---|
public static final Expression.ExpressionType ARRAY_ELEMENT_ACCESS
'AnyArray[offset]'
.
public static final Expression.ExpressionType ARRAY_TYPE_DECLARATOR
'AnyArray[]'
.
public static final Expression.ExpressionType BINARY_OPERATOR_EXPRESSION
Examples for such expressions are assignment expressions, shift expressions, comparison expressions and so on. I.e. all expressions with one operator and an operand on the left and right side of that operator must be marked by this constant.
public static final Expression.ExpressionType CLASS_CONSTRUCTOR_CALL
'new AnyType(constructorArgs)
.
STATIC_ARRAY_CREATOR
public static final Expression.ExpressionType CONDITIONAL_EXPRESSION
public static final Expression.ExpressionType DOT_EXPRESSION
DotExpression
expression types, i.e. dot
separated primary expressions
public static final Expression.ExpressionType EXPLICIT_CONSTRUCTOR_CALL
this
or super
constructor call expressions.
public static final Expression.ExpressionType IDENTIFIER
An identifier expression is nothing else than a not qualified identifier.
public static final Expression.ExpressionType INSTANCEOF_EXPRESSION
instanceof
expressions.
public static final Expression.ExpressionType KEYWORD
class
, this
, super
and void
.
public static final Expression.ExpressionType LITERAL
public static final Expression.ExpressionType METHOD_CALL
public static final Expression.ExpressionType PARENTHESIZED_EXPRESSION
public static final Expression.ExpressionType STATIC_ARRAY_CREATOR
'new AnyType[expression]'
or
'new AnyType[] {anyInitializers}'
.
CLASS_CONSTRUCTOR_CALL
public static final Expression.ExpressionType TYPE_CAST
public static final Expression.ExpressionType UNARY_OPERATOR_EXPRESSION
Examples for such expressions are pre/post increment/decrement expressions.
| Method Detail |
|---|
public static Expression.ExpressionType[] values()
for (Expression.ExpressionType c : Expression.ExpressionType.values()) System.out.println(c);
public static Expression.ExpressionType valueOf(java.lang.String name)
name
- the name of the enum constant to be returned.
java.lang.IllegalArgumentException
- if this enum type has no constant
with the specified name
java.lang.NullPointerException
- if the argument is null
|
||||||||||
| PREV CLASS NEXT CLASS | FRAMES NO FRAMES | |||||||||
| SUMMARY: NESTED | ENUM CONSTANTS | FIELD | METHOD | DETAIL: ENUM CONSTANTS | FIELD | METHOD |


Bootstrap Components - Part 7: List Groups
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How proteins “control” metal ions. Rigid protein structures (e.g. β-sheets) can confer strain on the metal, forcing it to adopt geometry of the transition state for the reaction it undergoes.
“Entasis” is the Greek word for stretched, which gives us the clue that its effect is structural. It in fact relates to distortion of coordination geometries around the metal ion(s) in a protein, and has been proven to exist by a variety of structural studies, namely EPR and Mossbauer Spectroscopy. It can also be elucidated from general redox properties.
It occurs because of and is related to the catalytic efficiency of the enzyme, and that the protein can fold to generate special stereochemistries which help the metal to adopt a geometry closer to that in the Transition State of the reaction.
It is seen in many enzymes. It has been most studied in “blue” Copper centres, where Cu(I) is seen to not adopt the expected perfect Tetrahedral geometry, and Cu(II) does not adopt a perfect square planar arrangement either. These blue Cu centres are found in a variety of electron transfer proteins and oxidases, such as azurin, plastocyanin and cytochrome c oxidase. The purpose is to enforce minimal difference between Cu(II) and Cu(I) geometries, i.e. the active site is held in an entatic state to minimize the reorganization energy. This allows for extremely fast electron transfer.
Other examples of its presence are seen around zinc in Carbonic Anhydrase and carboxypeptidase (distorted tetrahedra), and also iron in ferrodoxins. It is not easily modelled with simple ligands - no pre-organised strain.
X-ray Diffraction - protein structure and position of Metals (and separations if more than one). Poor at distinguishing metal atoms and diatomic ligands are hard to see. For this, use IR Spectroscopy.
EPR Spectroscopy - very useful for studying metal ions. Need them to be paramagnetic (odd electron) metals (S = n/2). Process is similar to NMR. Gives electron configuration information, and also shows any magnetic coupling.
Mossbauer Spectroscopy - good for Iron coordination chemistry generally. A 57Co source decays by electron capture to give an excited state 57Fe**. This then decays either straight to ground state (9%) or to a lower excited state (57Fe* - 91%). The energy gap between the ground and 1st excited is ∆E, and resonance is achieved by moving the Co source away from the 57Fe in the sample under test (57Fe is 2% abundant).
Cyclic Voltammetry - this can be used to study redox active centres, e.g. blue Cu centres.
These are used in Fe and Co (B12).
Note the delocalised π-system, and also that there is still the potential for two extra axial ligands to bind above and below the ring. This can carry Fe(II), (III) or (IV), although the latter is as FeIV=O (in biological systems only).
They find roles in electron transfer, ligand binding and catalysis.
Fe(III) + e- <=> Fe(II)
Eo ranges from +0.4 to -0.4 V depending on the ligands and the environment. Rates are determined by Marcus Theory - particularly the driving force, reorganisation energy and electronic coupling.
The heme ring ensures that the iron is always low spin, which accelerates the reaction greatly. It also acts as an electron antenna:
Cytochrome c is the classic example -
It occupies a position in chain of different cytochromes, and the whole process catalyses the formation of ATP from ADP:
NAD+ --> Flavoprotein --> Cyt b --> Cyt c1 --> Cyt c Æ Cyt c oxidase --> O2
It has Iron coordinated by a heme + two strong field ligands (Histidine and Methionine), so the iron is in its low spin configuration. This is advantageous for electron transfer as t2g6 <--> t2g5 (outer sphere) exchange will be far easier than any involving antibonding eg orbitals (the latter would require more distortion of the coordination sphere according to Marcus Theory, which expends energy and therefore slows the reaction).
Analysis of the crystal structure of cytochrome c containing both Fe(III) and Fe(II) has been accomplished. The structures are almost identical, which is further indication that the process is very fast, as a lack of change in conformation is ideal according to the Franck-Condon Principle (that is that electron transfer must occur between complexes of the same energy). This means that there is no need to adjust bond lengths between the two forms so that their energies are equivalent, i.e. that the free energy of reorganisation is very small. This results in very fast reactions according to Marcus Theory.
The structure also indicates that the iron is fully coordinated. This shows that the protein’s sole role is for electron transfer - no other reactions occur at its active site. This also renders it immune to other complexing ligands that may be toxic, e.g. cyanide, which deactivates cytochrome a. Another advantageous property is that the reaction is very clean. There are no other side-reactions and no harmful by-products or hazardous O-intermediates.
The mechanism by which the enzyme moves between the reductase (Cyt c1) and the oxidase (Cyt c oxidase) is not well understood. It is believed that when docking with the reductase, an electron is donated which is passed to the heme ring by π-electron cloud overlap, which gives rise to an ion pair. The fact that this is in a hydrophobic environment means that this is a very high energy intermediate, and this drives a conformational change that allows the electron to be shuttled between parallel residues, and compacts the protein and move to the oxidase.
Oxygen carrier. O2 binds end-on, and bent. It is also diamagnetic (i.e. the spins have been rearranged). Pauling explained this by considering singlet O2 binding to low spin Fe(II), such that the occupied π* on O2 acts as a σ-donor, and the empty π* acts as a π-acceptor. This gives the bent configuration.
Simple iron porphyrins do not show reversible ligand binding, as steric hindrance is required to stop oxidation.
Fe(III) and Fe(II) are connected by S2-. It is thus a mixed-valence compound.
Fe is usually found in tetrahedral geometry, and is high spin.
The clusters coordinate to proteins by thiolate ligands (Cysteine) to the Fe.
The most common ones are:
Super-clusters are also known, e.g. 8Fe-7S in nitrogenase.
The primary uses of these is in electron transfer, particularly for systems lying at the reducing end of process, i.e. e-transfer to/from enzymes that catalyse NADH/NAD+ and H+/H2 processes, e.g. Cytochrome P450.
Detection of the clusters is achieved by EPR or Mossbauer Spectroscopy. This gives information about Oxidation States and any magnetic interactions between Fe (ferromagnetic or antiferromagnetic coupling).
It is possible to make synthetic analogues under anaerobic and non-aqueous conditions, by using thiol ligands.
Ferredoxins - small proteins (MW ~ 12000), which carry ~2 clusters. They are essentially electron-carriers. Typically these are [3Fe-4S] and [4Fe-4S].
Hydrogenase - large protein (MW ~ 94000), which arrange the clusters in a line (wire-like) near the active site (NiFe). Thus sets up a chain of electron carriers.
Clusters are unstable with respect to Fe-O coordination (i.e. oxidation). They can be reformed by reduction though. These types of reaction are the basis by which a cell senses concentrations of Fe or O2 (relevant to protein production). Thus, FeS clusters transform in the presence of O2 or Fe which then alters the shape of the protein, and this then affects the binding of RNA/DNA.
This catalyses the isomerisation of citrate to iso-citrate in the Citric Acid cycle, by moving the OH between C atoms. This isomerisation does not require Co-B12.
It uses a [4Fe-4S] cluster, and works by coordinating the substrate, polarising the bond, and then rearranging, all at a specific iron site. This shows the role of Fe(III) as a strong Lewis Acid. Under aerobic conditions, the enzyme is inactive as [3Fe-4S]. On reduction, it forms the cubane cluster, and is active.
N2 + 8H+ + 8e- + 32ATP --> 2NH3 + H2 + 32ADP + 32HPO42-
The problem with this process is the energetics - there is a large activation energy to reach the LUMO and N2 has a triple bond.
Nitrogenase achieves this, but requires a lot of ATP to do it. It is in fact a 2-protein enzyme. The smaller part has a 4Fe-4S cluster which binds to ATP. The larger part is a dimer with 2 super- clusters - [8Fe-7S] (“P cluster”) and [Mo7Fe-8S-X]. The latter has a cage like structure, and it has recently been found that there is an X atom inside, which is believed to be an N in a resting (intermediate) state, i.e. as a µ6-nitride.
Catalyses H2 oxidation in some bacteria, which use H2 as a fuel. It is very active, and may be able to replace Pt as a catalyst for hydrogenation. This is an example of an Ni,Fe/RS cluster.
Fe(IV)=O is particularly relevant here, as it is strongly oxidising. It can be used as part of the O2 --> 2H2O process, and also in steroid synthesis and destroying toxins.
The classic example of Iron catalysis is Cytochrome P450:
These are glycoproteins, MW ~ 80000. There are 2 separate and approximately equivalent Fe binding sites.
They complex Fe(III) (which is hazardous when free), with simultaneous binding of HCO3- or CO32-, and release of H+. KA for the process is about 1023, but this is highly pH dependent, which controls the uptake.
A conformational change occurs on binding, locking the Fe(III) in due to the loss of internal mobility.
To release it again, the pH must drop, and something must be present to pick up the Fe(III) as it leaves. This is a chelator, such as siderophores, or a transferrin receptor on the cell surface (which then enters by exocytosis).
This stores non-heme iron in animals. It can carry 20% Fe by mass! It is a very large (MW 460000 - 550000) spherical protein, and is present in all types of organism. In mammals, it is typically found in the spleen and blood.
It is made up of 2 components - a “mineral” core (up to 4500 Fe atoms) and a protein shell. The 24 subunits that make it up link together like a soccer ball into a hollow sphere. Each subunit has 4 long α-helices and 1 short one, and then an anti-parallel β-sheet.
The mineral core comprises hydrated Fe(III) oxide + phosphate. It resembles 5Fe2O3.9H2O, with a HCP array of O and OH, with Fe3+ in the octahedral and tetrahedral holes. There is significant antiferromagnetic coupling. We cannot currently see where the phosphates are in relation to this (transparent to X-rays due to random ordering).
The iron enters and leaves through a controlled process:
2Fe(II) + O2 + 2H+ <=> 2Fe(III) + H2O2
This reaction occurs via an inner-sphere electron transfer mechanism at ferroxidase centres. Oxidation allows the iron to enter, while reduction allows it to leave.
Copper has useful redox properties, although for this reason it is extremely toxic when not bound to ligands. It usually binds to two histidine ligands, and then a cysteine if taking part in electron transfer. The maximum coordination is usually 5. There are no macrocyclic ligands known for it. Generally it is extracellular (unlike Fe) - presumably due to its toxicity. Also it appeared later in evolution due to solubilities relative to Fe.
This is very fast, as Cu(II)/Cu(I) are in the same geometries due to the entatic state.
Trigonal pyramidal geometry is usually seen, with 3 close equatorial ligands (2xHis + Cys) and then 2 axial (Gly and Met usually).
Binuclear Cu2 centres have been discovered in cytochrome c oxidase and N2O reductase. These were determined by spectroscopic and X- ray data.
It is believed to act as a relay centre (for e-transfer).
Hemocyanin (in arthropods and molluscs) has a binuclear Cu site too. It binds O2 reversibly (as in haemoglobin) although it is much harder to remove, and therefore a higher energy process. It is generally used for organisms where O2 is scarce (aquatic environments, for example) where as much O2 has to be taken in as possible.
O2 only binds to the Cu(I) form. However, charge transfer onto O2 occurs, so Cu(II) forms. This also gives rise to the blue colour.
This turns poly-ols into poly-als on the skins of fruit, via a poly-ol radical. This product then polymerises to protect the fruit from O2.
The active site is a trinuclear Cu centre, with a blue Cu centre near the surface that supplies the former with electrons.
This is found in the inner mitochondrial membrane, and is vital for aerobic organisms. It catalyses the reaction O2 --> 2H2O using 4 electrons, which come from oxidation of “CHO” and are delivered by Cytochrome c.
The active site is like a cross between haemoglobin and half haemocyanin.
It works with no harmful O-intermediates, and the energy released is used efficiently to pump H+, which sets up a gradient that drives ATP formation from ADP).
This is a cobalt-containing cofactor, and catalyses specific radical-based organic reactions (e.g. isomerisations) when bound to the appropriate enzyme.
It is a macrocyclic complex with a Co-alkyl bond. It is also the only known biologically active role for Cobalt, and one of very few organometallic compounds in nature.
It can only be synthesised by micro-organisms, but humans require trace amounts.
The macrocycle is a corrin ring - this is similar to the porphyrin, but only has 15 sides instead of 16. It also then coordinates an N-ligand (dimethyl benzimidazole) and 5’-deoxyadenosine by C (this is replaced by -CN for ingestion).
There are 3 oxidation states possible for the cobalt, all of which are low spin. CoII has an unpaired electron in a dz2 orbital (shown by EPR), which is the key to its catalytic properties.
Zn(II) is good because it binds strongly to proteins, while allowing rapid ligand exchange (e.g. for H2O or substrate). It also has good electron affinity and flexible geometry, with no redox chemistry troubles.
This helps biology find away round the need for strong H+/-OH to catalyse reactions (which would lead to hydrolysis of most biological compounds!).
Zn-carbonyl mechanism:
Zn-hydroxide mechanism:
CO2 + 2H2O <=> HCO3- + H3O+
Turnover of CO2 in biological systems is high, but solubility (this equilibrium) is very slow, and needs to be catalysed.
CA II has a MW ~ 30000, and is found in red blood cells. It carries this out at 106s-1, and is one of the most active of all enzymes.
The geometry around Zinc is a distorted tetrahedron, with 3 His ligands and OH2. It operates by the Zn-hydroxide mechanism, and delivers OH into CO2.
Carries out peptide hydrolysis. There are 2 types of Zn (A & B). B acts on basic residues, while A acts on C-terminal amino acids, and is thus easier to study.
CPD A has a MW of 34600. The Zn is found in one side of the groove where the substrate binds, and is coordinated by 2 x His, water, and a Glu residue (bidentate). It can however go up to 6 coordinate, e.g. when the inhibitor glycyl-L-tyrosine binds (with NH2 and carbonyl-O).
MW ~ 80000. Oxidises primary and secondary alcohols to aldehydes / ketones. Uses NAD+ as e-/H+ acceptor, and so is a redox enzyme. The Zinc activates the substrate for reaction with the cofactor. A subunit has two Zn atoms - one catalyses while the other stabilises the structure. Catalytic Zn has 2xCys + His + H2O coordination, while the structural Zinc has 4xCys protein ligands bound to it.
Hydrolyses phosphate esters (inc. ATP), and works best under mild alkali conditions.
R-OPO32- + H2O --> ROH + HOPO32-
It is a dimer, and each subunit has two Zn atoms in close proximity. The Phosphate then bridges the 2 Zn atoms. The other ligands are His and Asp.
Molecular Weight of ~ 17000. Has four Ca2+ binding sites in 2 pairs, at each end of a long molecule. Folds are called “EF Hands”. Kd for binding: 10-5-106 mol dm-3.
The binding alters the conformation, therefore it is recognised by enzymes (protein kinases). These are then activated to catalyse the phosphorylation of proteins.
Discuss the validity of the statement “Cytochrome c is perfectly designed for rapid electron transfer”.
Cytochromes are heme proteins which act as 1 electron carriers. They are found in all forms of aerobic life, as they are essential for the transformation of O2 into water, which drives the formation of ATP (the energy source of aerobic organisms) by a proton gradient across a membrane.
They can be tailored to suit the environments they are placed in by the organism, and broadly speaking there are 4 groups, labelled a-d. Cytochrome c features covalent links between the heme group and the protein, and is one of the best characterised and most studied of all enzymes due to the fact that it is readily soluble from the membrane.
Cytochrome c occupies a position in chain of different cytochromes, and the whole process catalyses the formation of ATP from ADP. The chain is something like this:
NAD+ --> Flavoprotein --> Cyt b --> Cyt c1 --> Cyt c --> Cyt c oxidase --> O2
It also has two strong field ligands (Histidine and Methionine), so the iron is in its low spin configuration. This is advantageous for electron transfer as t2g6 <--> t2g5 (outer sphere) exchange will be far easier than any involving antibonding eg orbitals (the latter would require more distortion of the coordination sphere according to Marcus Theory, which expends energy and therefore slows the reaction).
Analysis of the crystal structure of cytochrome c containing both Fe(III) and Fe(II) has been accomplished. The structures are almost identical, which is further indication that the process is very fast, as a lack of change in conformation is ideal according to the Franck-Condon Principle (that is that electron transfer must occur between complexes of the same energy). This means that there is no need to adjust bond lengths between the two forms so that their energies are equivalent, i.e. that the free energy of reorganisation is very small. This results in very fast reactions according to Marcus Theory.
Outer Sphere - energy terms:
Form Encounter Complex Æ Reorganisation Energy + ∆G for the process.
The initial formation of the encounter complex is essentially protein chemistry, and irrelevant of the metal ion. The reorganisation energy is the key, and is governed by Marcus Theory (self-exchange rates and equilibrium constant (∆G)). It is composed of ligand and solvent reorganisations.
The ligand reorganisation depends on both covalent (CFSE) and ionic (charge) contributions, while the solvent reorganisation depends on charge and ligand size (latter affects the size of the hydration sphere).
Cytochrome is almost perfectly designed to maximise these effects. It has large, fixed ligands (heme) which greatly reduce the solvent reorganisation energy term. The ligands are also uncharged for this also. The t2g6 <--> t2g5 exchange also is a non-bonding exchange, therefore less covalent effects in operation. Thus, the only ligand reorganisation is monopolar/dipolar axial ligands.
In terms of catalytic activity then, we can expect the rate to be very fast. This is enhanced by the π-system (porphyrin + phenylalanine close by). Recent evidence has suggested that this is not actually completely necessary though. A side-effect of this is that the electron transfer occurs over some distance, and it would be more efficient to have the transfer occurring between species as close as possible to each other (e.g. iron clusters). This then becomes a balance between reorganisation energy of ligands and close site transfer.
∆G is also important to consider. We want to minimise this, as we need to go down an energy gradient at the correct rate to pump protons most efficiently. The key point is not speed - thermodynamic constraint within which we want to go as fast as possible.
The structure also indicates that the iron is fully coordinated. This shows that the protein’s sole role is for electron transfer - no other reactions occur at its active site. This also renders it immune to other complexing ligands that may be toxic, e.g. cyanide, which deactivates cytochrome a. Another advantageous property is that the reaction is very clean. There are no other side-reactions and no harmful by-products or hazardous O-intermediates.
The mechanism by which the enzyme moves between the reductase (Cyt c1) and the oxidase (Cyt c oxidase) is not well understood. It is believed that when docking with the reductase, an electron is donated which is passed to the heme ring by π-electron cloud overlap, which gives rise to an ion pair. The fact that this is in a hydrophobic environment means that this is a very high energy intermediate, and this drives a conformational change that allows the electron to be shuttled between parallel residues, and compacts the protein and move to the oxidase.
Hence I would conclude that cytochrome c is perfectly designed for the role it carries out. It is fast and efficient and able to transfer large amounts of energy in a controlled manner over long distances. It’s only fault therefore would be that it requires many other components and enzymes in the electron transfer chain to be functioning correctly as well for it to actually be useful.
Compare and Contrast the roles of Fe and Cu in (i) Oxygen Binding Proteins, and (ii) Oxidases
Iron has two oxidation states in solution, Fe(II) and Fe(III). Ferrous ions are less common as it is easily oxidised to ferric. Most of the iron in humans is found at the centre of haemoglobin molecules, although some is stored in the liver and the rest used in redox reactions and protein formation in the plasma. The type of ligands attached greatly affects the properties (as would be expected). Typically, it is found as divalent (haemoglobin), trivalent (catalases and oxidases) or oxidised and reduced between both states (cytochromes).
Copper is also found in two different oxidation states, cuprous (I) and cupric (II). The former is easily oxidised to the latter in the same way as for iron. Cu(I) usually has coordination numbers equal to or less than 4, while Cu(II) reaches 6 (albeit Jahn-Teller distorted) and is rarely below 4. Next to iron, cupric is the best catalyst in oxidation-reduction processes. It is found in enzymes such as phenolase or hemocyanin, and these carry oxygen in the same way as haemoglobin. It is also required in the production of haemoglobin.
Fe tends to be found inside cells, while many Cu-containing enzymes are extracellular. Cu appeared in evolution far later than Fe, probably due to its greater availability in an aerobic environment (Cu2+ more soluble than Cu+, but Fe3+ are less soluble than Fe2+).
Fe is usually found inside a porphyrin-type macrocycle below.
Cu is rarely found in macrocyclic ligands, and tends to favour coordination by two or more Histidine ligands, and often a cysteine in electron transfer reactions. This reflects its “softer” chemical nature (i.e. bonding shows a higher degree of covalency and overlap).
Reversible Ligand Binding is achieved by the O2 molecule binding to the Fe end-on, in a bent configuration. The diamagnetism of the complex to Fe(II) indicates that there is a rearrangement of spins. This has been suggested as singlet O2 bound to low-spin Fe(II), with strong preference over Fe(III). The complex becomes bent as the occupied π*-orbital on O2> donates and the empty π*-orbital accepts. It should be noted though that simple Fe-porphyrin compounds do not exhibit reversible O2 binding, as steric hindrance is required to prevent oxidation.
For copper-based reversible O2 carriers such as haemocyanin, a binuclear Cu site is often seen.
O2 is bound reversibly as in haemoglobin. Binding will only occur to the Cu(I) form, but there is extensive charge transfer onto O2 so that the two Cu atoms are oxidised to Cu(II). This gives it a blue appearance.
The Fe-O2 bond is weaker than the Cu-O2 bond. This is a good thing in an O2 rich environment to maximise unloading potential (i.e. need to be able to pick up and release it as efficiently as possible). Cu is generally found when less O2 is available, e.g. in water organisms. This is because they need to pick up O2 whenever they can. Hence they develop a mechanism for removing it from the Cu binding site, which occurs at a higher ∆G. This is wasteful of energy, unless it is necessary for their survival (hence it is not used in humans). Also, Cu is poisonous if not handled carefully by the process.
Electron Transfer reactions are similar to those seen for ordinary complexes, and the rates are governed by Marcus Theory. Thus, importance factors are the driving force, reorganisation energy and electronic coupling between donor and acceptor sites.
Electron Transfer chemistry requires the full range of electrode potentials in order to function, e.g. the electron transport chain starts at negative potentials and works its way up to positive potentials. This optimises Eo for the process. Hence, both Fe and Cu find roles in it, as they have potentials that are optimal for different portions of the chain. Eo(Fe2+/Fe3+) = +0.77V, while Eo(Cu+/Cu2+) = +1.1V. Hence, Cu(I) can perform O2 chemistry, and finds many of its uses in oxidases (see below). The only way for Fe to have enough potential to do this would be if it were the Fe3+/Fe4+ couple. This is also used sometimes, e.g. cytochrome P450 which uses the iron(IV) oxo complex. However, Iron(II) is used for more negative Eo processes in the Electron Transport Chain (i.e. near the start).
For iron, the porphyrin macrocycle serves as an electron antenna:
Particular examples of this would be the cytochromes (cytochrome c discussed earlier).
However, there is also a range of iron-sulphur cluster proteins, which are found in all living organisms, where they are involved in a wide range of electron transfer processes. The iron is bound by sulphur atoms, either from cysteinyl residues or by inorganic sulphide., and there are a considerable range of structural types. Examples of some of the geometries possible are shown on the left.
Copper electron transfer proteins usually involve “blue” Cu centres. These can also transfer electrons at very high rates. The protein enforces the same geometry on the Cu irrespective of whether it is Cu(II) or Cu(I), so the reorganisation energy is very small.
Oxidases typically show a range of Cu centres. Iron’s role is usually involved in electron transfer as discussed above.
The Cu centres can come in many forms, e.g. ascorbate oxidase has a trinuclear centre, which is supplied with electrons by long-range transfer from a blue Cu centre close to the enzyme’s surface.
Cytochrome c oxidase is however the most famous oxidase involving copper. It is found in the inner mitochondrial membrane and catalyses 4 electron reduction of O2 to two H2O. It is essential to all higher forms of life as it enables the use of O2 as an oxidant.
The site of O2 reduction has a Cu atom close to an Fe porphyrin. It basically resembles a cross between the active site of haemoglobin and one half of the active site of haemocyanin.
Thus, Fe and Cu are involved in the redox cycle:
In conclusion, both these elements show electron-transfer like properties on account of the sensitive equilibrium between the Fe(II)/Fe(III) and the Cu(I)/Cu(II) states respectively. They are also both capable of binding to O2, and thus provide a mechanism for O2 transport around organisms. Biologically the latter tends to be dominated by iron, probably because “it got there first” evolutionarily speaking, as a result of its solubility properties.
The coordination environments A to E sketched below are found for metal ions in certain proteins, and the two sites in E contain the same metal ion. Suggest which of the ions Mg2+, Ca2+, Fe3+ and Zn2+ is most likely to be associated with each environment, giving reasons for your choice. Note that one of the metal ions is found in more than one of these environments.
This is expected to be Ca2+, due to the high coordination number - Ca2+ is a large ion compared to the other metals (no d-block contraction) and so it can coordinate more ligands without excessive steric hindrance. Also, all the ligands bind through O, which suggests it is a hard ion (Ca2+ fits this assessment).
Group 1 & 2 metals --> maximum coordination limited by sterics as the only factors. Ionic Model.
This is certainly Zn2+, and this particular arrangement is seen in Carbonic Anhydrase.
The distorted tetrahedron reflects Zn2+ small size (it sees the full effect of d-orbital contraction) so it can only coordinate 4 ligands. It also binds to N preferably to O (slightly softer).
4s/4p involvement (like p-block) --> Td.
Can go 5-coordinate (no CFSE issue) and 6 coordinate only with very small ligands.
This is a perfectly regular 6-coordinate metal centre, with O-donor ligands. This is probably Mg2+, which is small, hard and polarising, and unlikely to distort (no d-electrons, so not redox catalyst).
Same argument as for A (Calcium). Ionic Model.
This is a typical arrangement for an Fe-S cluster. This particular one is 2Fe-2S. Tetrahedral coordination around Fe(III) or Fe(II). Electron Transfer catalyst. Increased covalency for S.
This is haemoerythrin, which indicates it is Iron.
N/O ligands favour 6 coordination (smaller).
5/7 coordination unfavourable - can’t maximise CFSE or covalent overlap.
Transition Metals are often governed by directional bonding and CFSE arguments, in addition to the electrostatic/steric arguments given by the Ionic Model.
Can control whether Mg2+ or Ca2+ binds in the same site. Obviously can make site too small for Ca2+ to fit in, but to stop Mg2+ entering Ca2+ site is more complex.
First we consider that the electrostatic (binding) potential varies as 1/r. Hence, with Mg2+ inside a cavity (with walls essentially oppositely charged), shifting the Mg2+ from the centre means that it will bind more strongly, due to the 1/r dependence (think about the graph - 2 points on either side of the mid-point have a larger total than 2 x mid-point). However, Mg2+ is much more greatly hydrated than Ca2+ (i.e. ∆Hhyd(Mg2+) >> ∆Hhyd(Ca2+), even though ∆Hbind for Mg2+ > Ca2+). Therefore make sure that binding energy doesn’t compensate for ∆Hhyd(Mg2+).


Do you remember the scenario?
If Mr Barnes's transaction is considered suspicious, what must done next?
Imagine you are an employee of Big Bank. One of your customers, Mr Barnes, has an account in the name of his car dealership business.
Today, Mr Barnes deposited $27,000 in cash in his business account. This was unusual for Mr Barnes. He usually deposits third-party cheques or has money electronically transferred into the business account by his customers or by credit card companies.
While conducting the transaction, Mr Barnes appears nervous. When you ask him about the transaction, he mumbles something about a new customer and changes the subject.


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By Tom Curry Here is a guide to the process by which Gov. Rod Blagojevich of Illinois might be removed from office Impeachment is the formal accusation of wrongdoing, lobbed by a legislative body against an executive branch official, such as a governor ...


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Publications
Mani U, S. AS, Goutham R. N. A, Mohan S. S (2017) SWI/SNF Infobase—An exclusive information portal for SWI/SNF remodeling complex subunits. PLoS ONE 12(9): e0184445. https://doi.org/10.1371/journal.pone.0184445
Alagu SankareswaranS, ArunGoutham R.N., SumaMohan S, In silico screening of cancer-associated mutations in the HSA domain of BRG1 and its role in affecting the Arp-HSA sub-complex of SWI/SNF, Computational Biology and Chemistry, Volume 77, December 2018, Pages 109-115, doi: 10.1016/j.compbiolchem.2018.07.001


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implements LoadMetadata.
|
class |
LoadFuncWrapper
Convenience class to extend when decorating a LoadFunc.
|
| Modifier and Type | Method and Description |
|---|---|
protected LoadFunc |
LoadFuncWrapper.loadFunc() |
| Modifier and Type | Method and Description |
|---|---|
protected void |
LoadFuncWrapper.setLoadFunc(LoadFunc loadFunc)
The wrapped LoadFunc object must be set before method calls are made on this object.
|
| Modifier and Type | Class and Description |
|---|---|
class |
AbstractAccumuloStorage
A LoadStoreFunc for retrieving data from and storing data to Accumulo
A Key/Val pair will be returned as tuples: (key, colfam, colqual, colvis,
timestamp, value).
|
class |
AccumuloStorage
Basic PigStorage implementation that uses Accumulo as the backing store.
|
| Modifier and Type | Class and Description |
|---|---|
class |
MergeJoinIndexer
Merge Join indexer is used to generate on the fly index for doing Merge Join efficiently.
|
| Modifier and Type | Field and Description |
|---|---|
protected LoadFunc |
PigInputFormat.RecordReaderFactory.loadFunc |
| Constructor and Description |
|---|
PigRecordReader(org.apache.hadoop.mapreduce.InputFormat<?,?> inputformat,
PigSplit pigSplit,
LoadFunc loadFunc,
org.apache.hadoop.mapreduce.TaskAttemptContext context,
long limit) |
| Modifier and Type | Method and Description |
|---|---|
LoadFunc |
POLoad.getLoadFunc() |
| Constructor and Description |
|---|
POLoad(OperatorKey k,
LoadFunc lf) |
| Constructor and Description |
|---|
SparkPigRecordReader(org.apache.hadoop.mapreduce.InputFormat<?,?> inputformat,
PigSplit pigSplit,
LoadFunc loadFunc,
org.apache.hadoop.mapreduce.TaskAttemptContext context,
long limit) |
| Constructor and Description |
|---|
POSimpleTezLoad(OperatorKey k,
LoadFunc loader) |
| Modifier and Type | Class and Description |
|---|---|
class |
HBaseStorage
A HBase implementation of LoadFunc and StoreFunc.
|
| Modifier and Type | Class and Description |
|---|---|
class |
AvroStorage
Pig UDF for reading and writing Avro data.
|
class |
BinStorage
Load and store data in a binary format.
|
class |
JsonLoader
A loader for data stored using
JsonStorage . |
class |
OrcStorage
A load function and store function for ORC file.
|
class |
ParquetLoader
Wrapper class which will delegate calls to parquet.pig.ParquetLoader
|
class |
PigStorage
A load function that parses a line of input into fields using a character delimiter.
|
class |
TextLoader
This load function simply creates a tuple for each line of text that has a
single chararray field that
contains the line of text.
|
class |
TrevniStorage
Pig Store/Load Function for Trevni.
|
| Modifier and Type | Class and Description |
|---|---|
class |
Storage
A convenient mock Storage for unit tests
|
| Modifier and Type | Class and Description |
|---|---|
class |
DefaultIndexableLoader
Used by MergeJoin .
|
class |
PoissonSampleLoader
See "Skewed Join sampler" in http://wiki.apache.org/pig/PigSampler
|
class |
RandomSampleLoader
A loader that samples the data.
|
class |
SampleLoader
Abstract class that specifies the interface for sample loaders
|
| Modifier and Type | Field and Description |
|---|---|
protected LoadFunc |
SampleLoader.loader |
| Modifier and Type | Class and Description |
|---|---|
class |
InterStorage
LOAD FUNCTION FOR PIG INTERNAL USE ONLY!
This load function is used for storing intermediate data between MR jobs of
a pig query.
|
class |
ReadToEndLoader
This is wrapper Loader which wraps a real LoadFunc underneath and allows
to read a file completely starting a given split (indicated by a split index
which is used to look in the List
|
class |
SequenceFileInterStorage
Store tuples (BinSedesTuples, specifically) using sequence files to leverage
sequence file's compression features.
|
class |
TFileStorage
LOAD FUNCTION FOR PIG INTERNAL USE ONLY! This load function is used for
storing intermediate data between MR jobs of a pig query.
|
| Modifier and Type | Method and Description |
|---|---|
DataBag |
PigFile.load(LoadFunc lfunc,
PigContext pigContext) |
| Constructor and Description |
|---|
ReadToEndLoader(LoadFunc wrappedLoadFunc,
org.apache.hadoop.conf.Configuration conf,
String inputLocation,
int splitIndex) |
ReadToEndLoader(LoadFunc wrappedLoadFunc,
org.apache.hadoop.conf.Configuration conf,
String inputLocation,
int[] toReadSplitIdxs)
This constructor takes an array of split indexes (toReadSplitIdxs) of the
splits to be read.
|
ReadToEndLoader(LoadFunc wrappedLoadFunc,
org.apache.hadoop.conf.Configuration conf,
String inputLocation,
int splitIndex,
String signature) |
| Modifier and Type | Method and Description |
|---|---|
static ResourceSchema |
Utils.getSchema(LoadFunc wrappedLoadFunc,
String location,
boolean checkExistence,
org.apache.hadoop.mapreduce.Job job) |
| Modifier and Type | Method and Description |
|---|---|
LoadFunc |
LOLoad.getLoadFunc() |
| Constructor and Description |
|---|
LOLoad(FileSpec loader,
LogicalSchema schema,
LogicalPlan plan,
org.apache.hadoop.conf.Configuration conf,
LoadFunc loadFunc,
String signature)
Used from the LogicalPlanBuilder
|
| Modifier and Type | Class and Description |
|---|---|
class |
AllLoader
The AllLoader provides the ability to point pig at a folder that contains
files in multiple formats e.g.
|
class |
CSVExcelStorage
CSV loading and storing with support for multi-line fields,
and escaping of delimiters and double quotes within fields;
uses CSV conventions of Excel 2007.
|
class |
CSVLoader
A load function based on PigStorage that implements part of the CSV "standard"
This loader properly supports double-quoted fields that contain commas and other
double-quotes escaped with backslashes.
|
class |
FixedWidthLoader
A fixed-width file loader.
|
class |
HiveColumnarLoader
Loader for Hive RC Columnar files.
Supports the following types: * Hive Type Pig Type from DataType string CHARARRAY int INTEGER bigint or long LONG float float double DOUBLE boolean BOOLEAN byte BYTE array TUPLE map MAP Partitions The input paths are scanned by the loader for [partition name]=[value] patterns in the subdirectories. If detected these partitions are appended to the table schema. For example if you have the directory structure: |
class |
HiveColumnarStorage |
class |
IndexedStorage
IndexedStorage is a form of PigStorage that supports a
per record seek. |
class |
MyRegExLoader |
class |
PigStorageSchema
Deprecated.
Use PigStorage with a -schema option instead
|
class |
RegExLoader
RegExLoader is an abstract class used to parse logs based on a regular expression.
|
class |
SequenceFileLoader
A Loader for Hadoop-Standard SequenceFiles.
|
class |
XMLLoader
Parses an XML input file given a specified identifier of tags to be loaded.
|
| Modifier and Type | Method and Description |
|---|---|
LoadFunc |
AllLoader.AllReader.prepareLoadFuncForReading(PigSplit split) |
| Modifier and Type | Class and Description |
|---|---|
class |
CombinedLogLoader
CombinedLogLoader is used to load logs based on Apache's combined log format, based on a format like
LogFormat "%h %l %u %t \"%r\" %>s %b \"%{Referer}i\" \"%{User-Agent}i\"" combined
The log filename ends up being access_log from a line like
CustomLog logs/combined_log combined
Example:
raw = LOAD 'combined_log' USING org.apache.pig.piggybank.storage.apachelog.CombinedLogLoader AS
(remoteAddr, remoteLogname, user, time, method, uri, proto, status, bytes, referer, userAgent);
|
class |
CommonLogLoader
CommonLogLoader is used to load logs based on Apache's common log format, based on a format like
LogFormat "%h %l %u %t \"%r\" %>s %b" common
The log filename ends up being access_log from a line like
CustomLog logs/access_log common
Example:
raw = LOAD 'access_log' USING org.apache.pig.piggybank.storage.apachelog.CommongLogLoader AS (remoteAddr,
remoteLogname, user, time, method, uri, proto, bytes);
|
class |
LogFormatLoader
This is a pig loader that can load Apache HTTPD access logs written in (almost) any
Apache HTTPD LogFormat.
Basic usage: Simply feed the loader your (custom) logformat specification and it will tell you which fields can be extracted from this logformat. For example: |
| Modifier and Type | Method and Description |
|---|---|
List<org.apache.hadoop.fs.FileStatus> |
PathPartitionHelper.listStatus(org.apache.hadoop.mapreduce.JobContext ctx,
Class<? extends LoadFunc> loaderClass,
String signature)
This method is called by the FileInputFormat to find the input paths for
which splits should be calculated.
If applyDateRanges == true: Then the HiveRCDateSplitter is used to apply filtering on the input files. Else the default FileInputFormat listStatus method is used. |
void |
PathPartitionHelper.setPartitionFilterExpression(String partitionFilterExpression,
Class<? extends LoadFunc> loaderClass,
String signature)
Sets the PARITITION_FILTER_EXPRESSION property in the UDFContext
identified by the loaderClass.
|
void |
PathPartitionHelper.setPartitionKeys(String location,
org.apache.hadoop.conf.Configuration conf,
Class<? extends LoadFunc> loaderClass,
String signature)
Reads the partition keys from the location i.e the base directory
|
Copyright © 2007-2017 The Apache Software Foundation


The editor for a regular expression is essentially just a single text field. Operators in a regular expression are the Kleene star (*), the ``or'' operator (+), parentheses are also usable, and concatenation is accomplished by making symbols adjacent.
To make expressions
for this program to work with,
type them in the field.
Adjacent symbols
imply concatenation.
No symbol is used.
Many or nothing,
Asterisk (*) is the Kleine star.
What precedes repeats.
Additionally,
if you want an "or" symbol
the plus (+) should be used.
Screaming nothingness,
exclamations (!) are special.
They act as lambda.
Formatting errors
will be reported to you
when you choose actions.


ADD NEW
LISTING
Condition
Expiry Date
Item
Amount
Category
Notes
Put In Date
Action
2020-1-20
Apple
4
Fruit
healthy food
2020-1-25
Banana
4
Fruit
healthy food


| MATLAB File Help: Stack/findprop | View code for Stack/findprop | Go to online doc for Stack/findprop | Default Topics |
findprop Find property of MATLAB handle object. p = findprop(H,'PROPNAME') finds and returns the META.PROPERTY object associated with property name PROPNAME of scalar handle object H. PROPNAME must be a string. It can be the name of a property defined by the class of H or a dynamic property added to scalar object H. If no property named PROPNAME exists for object H, an empty META.PROPERTY array is returned. Help for Stack/findprop is inherited from superclass handle
| Defining Class | handle |
| Access | public |
| Sealed | false |
| Static | false |


| as_overscope {rlang} | R Documentation |
These functions have been deprecated in rlang 0.2.0. Please use
as_data_mask()
and new_data_mask()
instead. We no longer
require the mask to be cleaned up so overscope_clean()
does not
have a replacement.
as_overscope(quo, data = NULL) new_overscope(bottom, top = NULL, enclosure = NULL) overscope_clean(overscope)
quo |
A quosure. |
data |
A data frame or named vector of masking data. |
bottom |
The environment containing masking objects if the data mask is one environment deep. The bottom environment if the data mask comprises multiple environment. If you haven't supplied |
top |
The last environment of the data mask. If the data mask
is only one environment deep, This must be an environment that you own, i.e. that you have
created yourself. The parent of |
enclosure |
The |
overscope |
A data mask. |


Changelog
Version 1
1.1.2
-
Pair#flip!
andTriplet#flip!
no longer returnself
. If you want to explicitly assign the return values to a new variable, you should use the non-bang version (flip
).
1.1.1
-
Now licensed with the MIT license.
1.1.0
-
Remove specs from gem build.
-
Changes to Triplet and Pair alike:
-
Contents (left, right, middle) are all now reader attributes. However, they can still be assigned and modified using the same = syntax.
-
New @frozen instance variable in Triplet and Pair.
-
New custom
#eql?
/#==
methods for proper equivalency checks. -
New
#frozen?
method to check if the object is frozen. -
New
#freeze
to freeze the object, as well as its left, right, and middle values. -
New
#left=
,#right=
, and#middle=
methods that raise a RuntimeError if the object is frozen. -
New
#clone
method for proper mutability/pointers.
1.0.0
-
Initial release.


Allegro.pas 5.2 alpha-2Units Class Hierarchy Classes, Interfaces, Objects and Records Types Variables Constants Functions and Procedures Identifiers |
Unit al5nativedlg
Description
Defines an API that allows to use native dialogs and menus in a cross-platform way. This includes message dialogs, file choosers, main menu and more.
You should not use these dialogs if your app is running in full-screen modes.
Note that this isn't integrated with VCL, CLX, LCL nor fpGUI packages. Integration isn't even planned.
Overview
Functions and Procedures
Types
Description
Functions and Procedures
FUNCTION al_init_native_dialog_addon: AL_BOOL; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Initialise the native dialog addon.
Returns
True on success, False on error.

See also
- al_init_native_dialog_addon
- Initialise the native dialog addon.
|
FUNCTION al_create_native_file_dialog (CONST initial_path, title, patterns: AL_STR; Mode: AL_INT): ALLEGRO_FILECHOOSERptr; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Creates a new native file dialog. You should only have one such dialog opened at a time.
Parameters
- initial_path
- The initial search path and filename. To start with a blank file name the string should end with a directory separator (this should be the common case).
- title
- Title of the dialog.
- patterns
- A list of semi-colon separated patterns to match. This should not contain any whitespace characters. If a pattern contains the '/' character, then it is treated as a MIME type (e.g. 'image/png'). Not all platforms support file patterns. If the native dialog does not provide support, this parameter is ignored.
- mode
- 0, or a combination (
OR ) of the following flags:
ALLEGRO_FILECHOOSER_FILE_MUST_EXIST If supported by the native dialog, it will not allow entering new names, but just allow existing files to be selected. Else it is ignored.
ALLEGRO_FILECHOOSER_SAVE If the native dialog system has a different dialog for saving (for example one which allows creating new directories), it is used. Else it is ignored.
ALLEGRO_FILECHOOSER_FOLDER If there is support for a separate dialog to select a folder instead of a file, it will be used.
ALLEGRO_FILECHOOSER_PICTURES If a different dialog is available for selecting pictures, it is used. Else it is ignored.
ALLEGRO_FILECHOOSER_SHOW_HIDDEN If the platform supports it, also hidden files will be shown.
ALLEGRO_FILECHOOSER_MULTIPLE If supported, allow selecting multiple files.
Returns
A handle to the dialog which you can pass to al_show_native_file_dialog to display it, and from which you then can query the results using al_get_native_file_dialog_count and al_get_native_file_dialog_path. When you are done, call al_destroy_native_file_dialog on it.
If a dialog window could not be created then this function returns Nil . |
FUNCTION al_show_native_file_dialog (display: ALLEGRO_DISPLAYptr; dialog: ALLEGRO_FILECHOOSERptr): AL_BOOL; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Shows the dialog window. The display may be Nil , otherwise the given display is treated as the parent if possible.
This function blocks the calling thread until it returns, so you may want to spawn a thread and call it from inside that thread.
Returns
True on success, False on failure.
See also
- al_create_native_file_dialog
- Creates a new native file dialog.
|
PROCEDURE al_destroy_native_file_dialog (dialog: ALLEGRO_FILECHOOSERptr); CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Frees up all resources used by the file dialog.
|
FUNCTION al_show_native_message_box (display: ALLEGRO_DISPLAYptr; CONST title, heading, str, buttons: STRING; flags: AL_INT): AL_INT; INLINE; |
|
Shows a native GUI message box. This can be used for example to display an error message if creation of an initial display fails. The display may be Nil , otherwise the given display is treated as the parent if possible.
The message box will have a single "OK" button and use the style informative dialog boxes usually have on the native system. If the buttons parameter is not an empty string, you can instead specify the button text in a string, with buttons separated by a vertical bar (|).
The flags available are:
ALLEGRO_MESSAGEBOX_WARN The message is a warning. This may cause a different icon (or other effects).
ALLEGRO_MESSAGEBOX_ERROR The message is an error.
ALLEGRO_MESSAGEBOX_QUESTION The message is a question.
ALLEGRO_MESSAGEBOX_OK_CANCEL Display a cancel button alongside the "OK" button. Ignored if buttons is not an empty string.
ALLEGRO_MESSAGEBOX_YES_NO Display Yes/No buttons instead of the "OK" button. Ignored if buttons is not an empty string.
al_show_native_message_box may be called without Allegro being installed. This is useful to report an error during initialisation of Allegro itself.
Example:
button := al_show_native_message_box (
display,
'Warning',
'Are you sure?',
'If you click yes then you are confirming that "Yes" '+
'is your response to the query which you have '+
'generated by the action you took to open this '+
'message box.',
'',
ALLEGRO_MESSAGEBOX_YES_NO
);
Returns
0 if the dialog window was closed without activating a button.
1 if the OK or Yes button was pressed.
2 if the Cancel or No button was pressed
If buttons is not an empty string, the number of the pressed button is returned, starting with 1.
If a message box could not be created then this returns 0, as if the window was dismissed without activating a button. |
FUNCTION al_open_native_text_log (CONST title: AL_STR; flags: AL_INT): ALLEGRO_TEXTLOGptr; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Opens a window to which you can append log messages with al_append_native_text_log. This can be useful for debugging if you don't want to depend on a console being available.
Use al_close_native_text_log to close the window again.
Parameters
- title
- Title of the dialog.
- flags
- One of:
ALLEGRO_TEXTLOG_NO_CLOSE Prevent the window from having a close button. Otherwise, if the close button is pressed, an event is generated; see al_get_native_text_log_event_source.
ALLEGRO_TEXTLOG_MONOSPACE Use a monospace font to display the text.
Returns
Nil if there was an error opening the window, or if text log windows are not implemented on the platform.
See also
- al_append_native_text_log
- Appends a line of text to the message log window and scrolls to the bottom (if the line would not be visible otherwise).
- al_close_native_text_log
- Closes a message log window opened with
al_open_native_text_log earlier.
|
PROCEDURE al_append_native_text_log (textlog: ALLEGRO_TEXTLOGptr; CONST str: AL_STR); CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Appends a line of text to the message log window and scrolls to the bottom (if the line would not be visible otherwise). A line is continued until you add a newline character.
If the window is Nil then this function will fall back to calling Write . This makes it convenient to support logging to a window or a terminal.
|
FUNCTION al_get_native_text_log_event_source (textlog: ALLEGRO_TEXTLOGptr): ALLEGRO_EVENT_SOURCEptr; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Get an event source for a text log window. The possible events are:
ALLEGRO_EVENT_NATIVE_DIALOG_CLOSE The window was requested to be closed, either by pressing the close button or pressing Escape on the keyboard. The user.data1 field will hold a pointer to the ALLEGRO_TEXTLOG which generated the event. The user.data2 field will be 1 if the event was generated as a result of a key press; otherwise it will be zero.
|
FUNCTION al_get_allegro_native_dialog_version: AL_UINT32; CDECL; EXTERNAL ALLEGRO_NATIVE_DLG_LIB_NAME; |
|
Returns the (compiled) version of the addon, in the same format as al_get_allegro_version.
|
Types
Generated by PasDoc 0.14.0.
|


Yiming Chu
Contact:
Phone:408-644-0227
<EMAIL_ADDRESS>Yiming Chu
- Currently I'm on my second year in Northeastern University. I'm majored in Computer Science.
- Prior to coming to the USA, I've been working as a mobile developer for 7 years in the industry. My prior job is Android development. Besides, I also have experience in iOS development and web development.
- I'm fond of music. Prior to coming to the USA, I owned a band and I played guitar and bass.
- I like sports, including but not limited to basketball, table tennis, football, jogging and so on.
- I've a pet cat whose name is little black, he is very cute and 5 years' old.


CEERS Team Members
The CEERS collaboration is comprised of 18 CoIs from 12 Institutions, and 100 collaborators from 10 countries.
The CEERS collaboration is diverse on many axes with demonstrated expertise in rapid delivery of high-level science products. Co-I's are identified in the team list below with *.
- PI: Steven Finkelstein, University of Texas at Austin
- Viviana Acquaviva, CUNY/Flatiron CCA
- Omar Almaini, University of Nottingham
- Ricardo Amorín, Universidad de La Serena
- Véronique BUAT, Laboratoire d'Astrophysique de Marseille
- Bren Backhaus, University of Connecticut
- Micaela Bagley, University of Texas at Austin
- Guillermo Barro, University of the Pacific
- Peter Behroozi, University of Arizona
- Eric Bell, University of Michigan
- Rachana Bhatawdekar, European Space Agency (ESA ESTEC)
- Laura Bisigello, INAF Bologna
- Fernando Buitrago, University of Valladolid
- Denis Burgarella, Laboratoire d'Astrophysique de Marseille
- Antonello Calabro, INAF - OAR
- Caitlin Casey, University of Texas at Austin
- Marco Castellano, INAF - Osservatorio Astronomico di Roma
- Seth Cohen, Arizona State University
- Christopher Conselice, Manchester Uni
- Kevin Cooke, University of Kansas
- Mike Cooper, University of California Irvine
- Asantha Cooray, University of California Irvine
- Luca Costantin, Astrobiology Center, Madrid, Spain
- Darren Croton, Swinburne University of Technology
- Emanuele Daddi, CEA Saclay
- Romeel Davé, University of Edinburgh
- Avishai Dekel, The Hebrew University of Jerusalem / UCSC
- *Mark Dickinson, NSF's NOIRLab
- David Elbaz, CEA Saclay
- Vicente Estrada-Carpenter, Texas A&M University
- Sandra Faber, University of California, Santa Cruz
- *Henry Ferguson, Space Telescope Science Institute
- Jesús Vega Ferrero, Instituto de Astrofísica de Canarias (IAC)
- Keely Finkelstein, University of Texas at Austin
- Adriano Fontana, INAF Rome Observatory
- Jonathan Freundlich, Observatoire astronomique de Strasbourg
- Ángela García-Argumánez, Universidad Complutense de Madrid (UCM)
- Jonathan Gardner, NASA's Goddard Space Flight Center
- Eric Gawiser, Rutgers University
- Mauro Giavalisco, University of Massachusetts Amherst
- *Andrea Grazian, INAF - Osservatorio Astronomico di Padova
- *Norman Grogin, Space Telescope Science Institute
- Timothy Hamilton, Shawnee State University
- Pablo Arrabal Haro, NSF's NOIRLab
- Nimish Hathi, Space Telescope Science Institute
- Benne Holwerda, University of Louisville
- Marc Huertas-Company, IAC - Observatoire de Paris
- Taylor Alexandra Hutchison, Texas A&M University
- Kartheik Iyer, Dunlap Institute for Astronomy & Astrophysics, University of Toronto
- Saurabh W. Jha, Rutgers University
- Shardha Jogee, University of Texas at Austin
- Stephanie Juneau, NSF's NOIRLab
- Intae Jung, NASA's Goddard Space Flight Center / CUA
- *Jeyhan Kartaltepe, Rochester Institute of Technology
- Susan Kassin, Space Telescope Science Institute
- *Lisa Kewley, Harvard-Smithsonian Center for Astrophysics
- Allison Kirkpatrick, KU
- *Dale Kocevski, Colby College
- *Anton Koekemoer, Space Telescope Science Institute
- Peter Kurczynski, NASA's Goddard Space Flight Center
- Jussi Kuusisto, University of Sussex
- Rebecca Larson, University of Texas at Austin
- Soo Lee, Purdue University
- Gene Leung, University of Texas at Austin
- *Jennifer Lotz, Gemini Observatory/NSF's NOIRLab
- Ray Lucas, Space Telescope Science Institute
- Kameswara Bharadwaj Mantha, University of Missouri Kansas City
- Jasleen Matharu, Texas A&M University
- Elizabeth McGrath, Colby College
- Daniel McIntosh, UMKC
- Emiliano Merlin, INAF
- Bahram Mobasher, University of California, Riverside
- Jeffrey Newman, University of Pittsburgh / PITT PACC
- David Nicholls, Australian National University
- Oscar A. Chavez Ortiz, University of Texas at Austin
- Camilla Pacifici, Space Telescope Science Institute
- Viraj Pandya, University of California Santa Cruz
- *Casey Papovich, Texas A&M University
- *Laura Pentericci, INAF - Osservatorio Astronomico di Roma
- *Nor Pirzkal, Space Telescope Science Institute
- *Pablo G. Pérez-González, Centro de Astrobiología (CAB/CSIC--INTA)
- Marc Rafelski, Space Telescope Science Institute
- *Swara Ravindranath, Space Telescope Science Institute
- Russell Ryan, Space Telescope Science Institute
- Paola Santini, INAF - Osservatorio Astronomico di Roma
- Ekta Shah, Rochester Institute of Technology
- Raymond Simons, Space Telescope Science Institute
- Gregory Snyder, Space Telescope Science Institute
- *Rachel Somerville, Flatiron Institute
- Elizabeth Stanway, University of Warwick, UK
- Amber Straughn, NASA's Goddard Space Flight Center
- Sandro Tacchella, Harvard-Smithsonian Center for Astrophysics
- Harry Teplitz, Caltech/IPAC
- *Jonathan Trump, UConn
- Brittany Vanderhoof, Rochester Institute of Technology
- Alexander de la Vega, Johns Hopkins University
- Weichen Wang, Johns Hopkins University
- Benjamin Weiner, Steward Observatory, U. of Arizona
- *Stephen Wilkins, University of Sussex
- Christopher Willmer, Steward Observatory/University of Arizona
- Isak Wold, NASA's Goddard Space Flight Center
- Stijn Wuyts, University of Bath
- Guang Yang, Texas A&M University
- L. Y. Aaron Yung, NASA's Goddard Space Flight Center
- Jorge Zavala, University of Texas at Austin


{% extends "base.html" %} {% block title %}
Medieval catalogues > UNIVERSITY AND COLLEGE LIBRARIES OF OXFORD > Magdalen College > List of donated books, probably by John Neele, 22 Aug. 1488 × 21 Aug. 1489
{% endif %}37 identified entries found.
All data was derived from the List of Identifications by Professor Richard Sharpe.
{% if not printing %}
A key to codes used in the List is available (opens in new tab).{% endif %}


In POSIX sh, name matching prefixes are undefined.
(or "In dash, ... are not supported." when using dash
)
#!/bin/sh
echo "${!ANDROID_*}"
The easiest solution is to switch to a shell that does support name matching prefixes, like bash
:
#!/bin/bash
echo "${!ANDROID_*}"
Alternatively, extract the data you want from env
or set
Using ${!name*}
to find all variable names with a given prefix is a bash and ksh extension that dash
and POSIX sh
does not support.
If you only intend to target shells that supports this feature, you can change the shebang to a shell that guarantees support, or [[ignore]] this warning.
You can use # shellcheck disable=SC3000-SC4000
to ignore all such compatibility
warnings.