Inter-ring rotation of apolipoprotein A-I protein monomers for the double-belt model using biased molecular dynamics》.pdfVIP

Journal of Molecular Graphics and Modelling 29 (2011) 1006–1014 Contents lists available at ScienceDirect Journal of Molecular Graphics and Modelling j o u rn al h omepage: w w w. elsev /locate/JMGM Inter-ring rotation of apolipoprotein A-I protein monomers for the double-belt model using biased molecular dynamics Thomas R. Caulfield ∗ School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0230, United States a r t i c l e i n f o a b s t r a c t Article history: The double belt model for lipid-bound discoidal apolipoprotein A-I consists of two alpha-helical Received 23 June 2010 monomers bound about an unilamellar bilayer of lipids. Previous work, based on salt bridge calcu- Received in revised form 29 March 2011 lations, has demonstrated that the L5/5 registration, Milano mutant, and Paris mutant are preferred Accepted 19 April 2011 conformations for apolipoprotein A-I. The salt bridge scoring indicated better energetic scoring in these Available online 27 April 2011 alignments. The Paris (R151C) and Milano (R173C) mutants indicate a mode of change must be available. To find proper registration, one proposed change is a ‘rotationally’ independent circular motion of the Keywords: two protein monomers about the lipid unilamellar bilayer core. Here, we present computational data for Apolipoprotein A-I Discoidal high density lipoprotein