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.
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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) |
@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} }