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oai:www.ideals.illinois.edu:2142/22296 2023-07-10 col_2142_5131 col_2142_8859 col_2142_14828 com_2142_5130 com_2142_8858 com_2142_234 com_2142_14827 com_2142_14793 com_2142_8903

Schulten, Klaus J. Zhou, Feng 2011-05-07T13:35:21Z 2011-05-07T13:35:21Z 10000-01-01 1996 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. Made available in DSpace on 2011-05-07T13:35:21Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9625221.pdf: 7704239 bytes, checksum: cfda38d1d28460daf9629006bd7953a9 (MD5) Previous issue date: 1996 Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:56:39Z Item is restricted indefinitely. Restriction data tranferred 2014-07-01T11:26:30-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission ETDs are only available to UIUC Users without author permission U of I Only AAI9625221 (UMI)AAI9625221 http://hdl.handle.net/2142/22296 eng Copyright 1996 Zhou, Feng Biology, Molecular Chemistry, Biochemistry Chemistry, Physical Molecular dynamics studies of membranes and membrane proteins text Biophysics and Computational Biology Biophysics and Computational Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.