Crossref journal-article
Wiley
Proteins: Structure, Function, and Bioinformatics (311)
Abstract

AbstractA 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.

Bibliography

Marques, O., & Sanejouand, Y. (1995). Hinge‐bending motion in citrate synthase arising from normal mode calculations. Proteins: Structure, Function, and Bioinformatics, 23(4), 557–560. Portico.

Authors 2
  1. Osni Marques (first)
  2. Yves‐Henri Sanejouand (additional)
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Dates
Type When
Created 20 years, 2 months ago (May 28, 2005, 9:48 p.m.)
Deposited 1 year, 10 months ago (Oct. 26, 2023, 7:43 p.m.)
Indexed 3 weeks, 6 days ago (July 30, 2025, 11:20 a.m.)
Issued 29 years, 8 months ago (Dec. 1, 1995)
Published 29 years, 8 months ago (Dec. 1, 1995)
Published Online 21 years, 6 months ago (Feb. 3, 2004)
Published Print 29 years, 8 months ago (Dec. 1, 1995)
Funders 0

None

@article{Marques_1995, title={Hinge‐bending motion in citrate synthase arising from normal mode calculations}, volume={23}, ISSN={1097-0134}, url={http://dx.doi.org/10.1002/prot.340230410}, DOI={10.1002/prot.340230410}, number={4}, journal={Proteins: Structure, Function, and Bioinformatics}, publisher={Wiley}, author={Marques, Osni and Sanejouand, Yves‐Henri}, year={1995}, month=dec, pages={557–560} }