Molecular dynamics studies of membranes and membrane proteins
Zhou, Feng
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https://hdl.handle.net/2142/22296
Description
Title
Molecular dynamics studies of membranes and membrane proteins
Author(s)
Zhou, Feng
Issue Date
1996
Doctoral Committee Chair(s)
Schulten, Klaus J.
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics and Computational Biology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Chemistry, Biochemistry
Chemistry, Physical
Language
eng
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.
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