Molecular dynamics simulations of GlpF in a micelle vs in a bilayer: conformational dynamics of a membrane protein as a function of environment.

Journal article

Octyl glucoside (OG) is a detergent widely employed in structural and functional studies of membrane proteins. To better understand the nature of protein-OG interactions, molecular dynamics simulations (duration 10 ns) have been used to explore an alpha-helical membrane protein, GlpF, in OG micelles and in DMPC bilayers. Greater conformational drift of the extramembraneous protein loops, from the initial X-ray structure, is seen for the GlpF-OG simulations than for the GlpF-DMPC simulation. T...

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Authors: Patargias, G; Bond, P; Deol, S; Sansom, MS

• Publication status: Published
• Journal: journal of physical chemistry. B
• Volume: 109
• Issue: 1
• Pages: 575-582
• Publication date: 2005-01-01
• DOI: 10.1021/jp046727h
• EISSN: 1520-5207
• ISSN: 1520-6106
• Language: English
• Keywords: Aquaporins; Time Factors; Membrane Proteins; Escherichia coli Proteins; Protein Conformation; Glucosides; Lipid Bilayers; Protein Structure, Secondary; Computer Simulation; Micelles; Structure-Activity Relationship; Models, Molecular