Document Detail

Insertion and assembly of membrane proteins via simulation.
MedLine Citation:
PMID:  16492056     Owner:  NLM     Status:  MEDLINE    
Interactions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, namely, glycophorin (a simple alpha-helical bundle) and OmpA (a beta-barrel). The accuracy of the coarse-grained simulations is established via comparison with the equivalent atomistic simulations of self-assembly of protein/detergent micelles. The simulation of OmpA/bilayer self-assembly reveals how a folded outer membrane protein can be inserted in a bilayer. The glycophorin/bilayer simulation supports the two-state model of membrane folding, in which transmembrane helix insertion precedes dimer self-assembly within a bilayer. The simulations also suggest that a dynamic equilibrium exists between the glycophorin helix monomer and dimer within a bilayer. The simulated glycophorin helix dimer is remarkably close in structure to that revealed by NMR. Thus, coarse-grained methods may help to define mechanisms of membrane protein (re)folding and will prove suitable for simulation of larger scale dynamic rearrangements of biological membranes.
Peter J Bond; Mark S P Sansom
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  128     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2006 Mar 
Date Detail:
Created Date:  2006-02-22     Completed Date:  2006-04-25     Revised Date:  2008-10-03    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2697-704     Citation Subset:  IM    
Department of Biochemistry, University of Oxford, UK.
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MeSH Terms
Bacterial Outer Membrane Proteins / chemistry*,  metabolism
Computer Simulation
Glycophorin / chemistry*,  metabolism
Lipid Bilayers / chemistry*,  metabolism
Models, Chemical
Models, Molecular
Protein Structure, Secondary
Grant Support
//Wellcome Trust
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Glycophorin; 0/Lipid Bilayers; 0/Micelles; 149024-69-1/OMPA outer membrane proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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