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Title:Molecular dynamics studies of membranes and membrane proteins
Author(s):Zhou, Feng
Doctoral Committee Chair(s):Schulten, Klaus J.
Department / Program:Biophysics and Computational Biology
Discipline:Biophysics and Computational Biology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Biology, Molecular
Chemistry, Biochemistry
Chemistry, Physical
Abstract:Properties of phospholipid membrane bilayers and of proteins associating and functioning in the membrane bilayer or at the membrane-water interface are studied by combining molecular dynamics simulations, free energy perturbation theory and continuum electrostatics calculations. Three systems were investigated: (1) The proton pump cycle of the integral membrane protein bacteriorhodopsin: The photoisomerization and subsequent thermal reactions of the protein were studied by molecular dynamics simulations. Internal water molecules were placed in the protein. The studies attribute a key role to the Schiff base-counterion electrostatic interaction in controlling the initial photoreaction and revealed an important role of internal water molecules for the function of bacteriorhodopsin. (2) A dilaurylphosphatidylethanolamine membrane bilayer solvated in excess water: Structural properties of the membrane, electrostatic properties of the membrane-water interface and charge distributions on the membrane surface were characterized. (3) The activation of enzyme human synovial phospholipase A$\sb2$ at membrane surface was investigated. The activation was attributed to desolvation effects of lipid head groups in a tight enzyme-membrane complex. The electrostatic interactions between the enzyme and the membrane were studied and found to favor the binding of negatively charged lipid molecules to the enzyme-membrane interface.
Issue Date:1996
Type:Text
Language:English
URI:http://hdl.handle.net/2142/22296
Rights Information:Copyright 1996 Zhou, Feng
Date Available in IDEALS:2011-05-07
Identifier in Online Catalog:AAI9625221
OCLC Identifier:(UMI)AAI9625221


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