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Hinge‐bending motion in citrate synthase arising from normal mode calculations
Author(s) -
Marques Osni,
Sanejouand YvesHenri
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230410
Subject(s) - hinge , normal mode , bending , citrate synthase , motion (physics) , path (computing) , amplitude , chemistry , physics , biophysics , crystallography , classical mechanics , enzyme , biochemistry , biology , thermodynamics , computer science , vibration , acoustics , optics , programming language
A normal mode 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 become useful for determining a first approximation of the conformational path between the closed and open forms of these proteins. © 1995 Wiley‐Liss, Inc.