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Bacteriorhodopsin α‐helices in lipid settings: Insights for structure prediction
Author(s) -
Woolf Thomas B.
Publication year - 1998
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/(sici)1097-461x(1998)69:1<105::aid-qua12>3.0.co;2-5
Subject(s) - bacteriorhodopsin , molecular dynamics , chemistry , folding (dsp implementation) , lipid bilayer , transmembrane domain , bilayer , protein folding , transmembrane protein , chemical physics , crystallography , biophysics , computational chemistry , membrane , biology , biochemistry , receptor , electrical engineering , engineering
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