1jxt: Difference between revisions

Revision as of 14:28, 21 February 2008

CRAMBIN MIXED SEQUENCE FORM AT 160 K. PROTEIN/WATER SUBSTATES

OverviewOverview

Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.

About this StructureAbout this Structure

1JXT is a Single protein structure of sequence from Crambe hispanica subsp. abyssinica with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

On the nature of a glassy state of matter in a hydrated protein: Relation to protein function., Teeter MM, Yamano A, Stec B, Mohanty U, Proc Natl Acad Sci U S A. 2001 Sep 25;98(20):11242-7. PMID:11572978

Page seeded by OCA on Thu Feb 21 13:28:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1jxt.jpg|left|200px]]<br /><applet load="1jxt" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jxt.jpg|left|200px]]<br /><applet load="1jxt" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jxt, resolution 0.89&Aring;" />
 '''CRAMBIN MIXED SEQUENCE FORM AT 160 K. PROTEIN/WATER SUBSTATES'''<br />
 ==Overview==
-Diverse biochemical and biophysical experiments indicate that all, proteins, regardless of size or origin, undergo a dynamic transition near, 200 K. The cause of this shift in dynamic behavior, termed a "glass, transition," and its relation to protein function are important open, questions. One explanation postulated for the transition is solidification, of correlated motions in proteins below the transition. We verified this, conjecture by showing that crambin's radius of gyration (Rg) remains, constant below approximately 180 K. We show that both atom position and, dynamics of protein and solvent are physically coupled, leading to a novel, cooperative state. This glassy state is identified by negative slopes of, the Debye-Waller (B) factor vs. temperature. It is composed of, multisubstate side chains and solvent. Based on generalization of, Adam-Gibbs' notion of a cooperatively rearranging region and decrease of, the total entropy with temperature, we calculate the slope of the, Debye-Waller factor. The results are in accord with experiment.
+Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.
 ==About this Structure==
-JXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica] with EOH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JXT OCA].
+JXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Crambe_hispanica_subsp._abyssinica Crambe hispanica subsp. abyssinica] with <scene name='pdbligand=EOH:'>EOH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXT OCA].
 ==Reference==
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 [[Category: Mohanty, U.]]
 [[Category: Stec, B.]]
-[[Category: Teeter, M.M.]]
+[[Category: Teeter, M M.]]
 [[Category: Yamano, A.]]
 [[Category: EOH]]
@@ Line 22: / Line 22: @@
 [[Category: water]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:40:29 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:00 2008''