1jmw

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(New page: 200px<br /><applet load="1jmw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmw, resolution 1.9&Aring;" /> '''Propagating Conformat...)
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[[Image:1jmw.jpg|left|200px]]<br /><applet load="1jmw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jmw.jpg|left|200px]]<br /><applet load="1jmw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jmw, resolution 1.9&Aring;" />
caption="1jmw, resolution 1.9&Aring;" />
'''Propagating Conformational Changes Over Long (And Short) Distances'''<br />
'''Propagating Conformational Changes Over Long (And Short) Distances'''<br />
==Overview==
==Overview==
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The problem of the propagation of conformational changes over long, distances or through a closely packed protein is shown to fit a model of a, ligand-induced conformational change between two protein states selected, by evolution. Moreover, the kinetics of the pathway between these states, is also selected so that the energy of ligand binding and the speed of the, transition between conformational states are physiologically appropriate., The crystallographic data of a wild-type aspartate receptor that has, negative cooperativity and a mutant that has no cooperativity but has, native transmembrane signaling are shown to support this model.
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The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.
==About this Structure==
==About this Structure==
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1JMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JMW OCA].
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1JMW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMW OCA].
==Reference==
==Reference==
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[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Jr., D.E.Koshland.]]
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[[Category: Jr., D E.Koshland.]]
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[[Category: Yu, E.W.]]
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[[Category: Yu, E W.]]
[[Category: bacterial chemotactic receptor]]
[[Category: bacterial chemotactic receptor]]
[[Category: chemotaxis]]
[[Category: chemotaxis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:23:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:25 2008''

Revision as of 11:24, 21 February 2008


1jmw, resolution 1.9Å

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Propagating Conformational Changes Over Long (And Short) Distances

Overview

The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.

About this Structure

1JMW is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Propagating conformational changes over long (and short) distances in proteins., Yu EW, Koshland DE Jr, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9517-20. PMID:11504940

Page seeded by OCA on Thu Feb 21 13:24:25 2008

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