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van der Spoel, David, de Groot, Bert L., Hayward, Steven 
ORCID: https://orcid.org/0000-0001-6959-2604, Berendsen, Herman J. C. and Vogel, Hans J.
(1996)
Bending of the calmodulin central helix: A theoretical study.
Protein Science, 5 (10).
pp. 2044-2053.
Abstract
The crystal structure of calcium-calmodulin (CaM) reveals a protein with a typical dumbbell structure. Various spectroscopic studies have suggested that the central linker region of CaM, which is α-helical in the crystal structure, is flexible in solution. In particular, NMR studies have indicated the presence of a flexible backbone between residues Lys 77 and Asp 80. This flexibility is related directly to the function of the protein because it enables the N- and C-terminal domains of the protein to move toward each other and bind to the CaM-binding domain of a target protein. We have investigated the flexibility of the CaM central helix by a variety of computational techniques: molecular dynamics (MD) simulations, normal mode analysis (NMA), and essential dynamics (ED) analysis. Our MD results reproduce the experimentally determined location of the bend in a simulation of only the CaM central helix, indicating that the bending point is an intrinsic property of the α-helix, for which the remainder of the protein is not important. Interestingly, the modes found by the ED analysis of the MD trajectory are very similar to the lowest frequency modes from the NM analysis and to modes found by an ED analysis of different structures in a set of NMR structures. Electrostatic interactions involving residues Arg 74 and Asp 80 seem to be important for these bending motions and unfolding, which is in line with pH-dependent NMR and CD studies.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Computing Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Computational Biology |
| Depositing User: | Vishal Gautam |
| Date Deposited: | 30 Jun 2011 09:26 |
| Last Modified: | 22 Apr 2023 23:56 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/23106 |
| DOI: | 10.1002/pro.5560051011 |
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