ISSN:
0020-7608
Keywords:
bacteriorhodopsin
;
protein: lipid interactions
;
α-helices
;
molecular dynamics
;
membrane protein tertiary structure prediction
;
Chemistry
;
Theoretical, Physical and Computational Chemistry
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The two-stage model of membrane protein folding predicts that isolated transmembrane α-helices form stably in the bilayer before coming together to form the fully functional protein. Insight into the molecular implications of this model are possible with detailed molecular dynamics calculations. Thirty molecular dynamics simulations of both individual and pairs of α-helices from bacteriorhodopsin were calculated with the CHARMm program. This data base will continue to grow and expand. Already, differences between identical helices in different media and different helices in the same media have been found. The current results are summarized in this contribution. © 1998 John Wiley & Sons, Inc. Int J Quant Chem 69: 105-116, 1998
Additional Material:
9 Ill.
Type of Medium:
Electronic Resource
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