| Hinge-Bending Motion in Citrate Synthase Arising from Normal Modes Calculations | |
Abstract/OtherAbstract
:
|
A normal modes analysis of the closed form of dimeric citrate synthase has been performed. The largest-amplitude collective motion predicted by this method compares well with the crystallographically observed hinge-bending motion. Such a result supports those obtained previously in the case of hinge-bending motions of smaller systems, such as lysozyme or hexokinase. Taken together, all these results suggest that low-frequency normal modes may happen to become useful for determining a first approximation of the conformational path between the closed and open forms of these proteins. Keywords: collective motion, normal modes analysis, low-frequency motion, hinge-bending, closed form of citrate synthase. Introduction In many proteins, large conformational transitions involve the relative movement of almost rigid structural elements. In citrate synthase, a two-domain protein, coenzyme A binding induces a 18 0 rotation of the small domain around an axis close to residue 274, which repre... |
Authors
:
|
Yves-henri Sanejou,Osni A. Marques,Yves-henri Sanejouand |
Contributors
:
|
The Pennsylvania State University CiteSeer Archives |
Publication Detail
:
|
Publisher : unknown Type : - Format : ps |
Date Detail
:
|
1995-11-17 |
Subject
:
|
Yves-henri Sanejou,Osni A. Marques,Yves-henri Sanejouand Hinge-Bending Motion in Citrate Synthase Arising from Normal Modes Calculations |
Coverage
:
|
- |
Relation
:
|
- |
Source
:
|
http://www.cerfacs.fr/algor/reports/TR_PA_95_31.ps.gz |
Copyright Information
:
|
unrestricted |
Other Details
:
|
Languages : en |
Export Citation
:
|
APA/MLA Format Download EndNote Download BibTex |
Previous Document: Somatic mutations in immunoglobulin V gene determine the structure and function of the protein - an ...
Next Document: PROver with a