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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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