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Hinge‐bending motion in citrate synthase arising from normal mode calculations
Abstract
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.
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Cited by
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Conformational change of proteins arising from normal mode calculations
Tama, F., & Sanejouand, Y.-H. (2001) · Protein Engineering, Design and Selection · doi:10.1093/protein/14.1.1 · Cited by 891
Self-citationNormal Mode Analysis of Biomolecular Structures: Functional Mechanisms of Membrane Proteins
Bahar, I., Lezon, T. R., Bakan, A., & Shrivastava, I. H. (2010) · Chemical Reviews · doi:10.1021/cr900095e · Cited by 537
Global ribosome motions revealed with elastic network model
Wang, Y., Rader, A. J., Bahar, I., & Jernigan, R. L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.01.005 · Cited by 284
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Metadata
- Authors
- Marques, O., & Sanejouand, Y.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 1995-12
- Volume
- 23
- Issue
- 4
- Pages
- 557-560
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2063962473
- Cited by
- 191
- References
- 0
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Open access
- closed
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- Marques, O., & Sanejouand, Y. (1995). Hinge‐bending motion in citrate synthase arising from normal mode calculations. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340230410
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