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Structural studies of membrane proteins have highlighted the likely influence of membrane mimetic environments (i.e., lipid bilayers versus detergent micelles) on the conformation and dynamics of small α-helical membrane proteins. We have used molecular dynamics simulations to compare the conformational dynamics of BM2 (a small α-helical protein from the membrane of influenza B) in a model phospholipid bilayer environment with its behavior in protein-detergent complexes with either the zwitterionic detergent dihexanoylphosphatidylcholine (DHPC) or the nonionic detergent dodecylmaltoside (DDM). We find that DDM more closely resembles the lipid bilayer in terms of its interaction with the protein, while the short-tailed DHPC molecule forms "nonphysiological" interactions with the protein termini. We find that the intrinsic micelle properties of each detergent are conserved upon formation of the protein-detergent complex. This implies that simulations of detergent micelles may be used to help select optimal conditions for experimental studies of membrane proteins.

Original publication

DOI

10.1021/jp505127y

Type

Journal article

Journal

J Phys Chem B

Publication Date

22/01/2015

Volume

119

Pages

764 - 772

Keywords

1,2-Dipalmitoylphosphatidylcholine, Detergents, Glucosides, Influenza B virus, Ion Channels, Lipid Bilayers, Micelles, Molecular Dynamics Simulation, Phosphatidylcholines, Porosity, Protein Binding, Protein Stability, Protein Structure, Secondary, Protons, Viral Proteins, Water