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William C. Wimley
Researcher at Tulane University
Publications - 150
Citations - 14450
William C. Wimley is an academic researcher from Tulane University. The author has contributed to research in topics: Lipid bilayer & Membrane. The author has an hindex of 49, co-authored 136 publications receiving 13201 citations. Previous affiliations of William C. Wimley include Johns Hopkins University & University Medical Center New Orleans.
Papers
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Journal ArticleDOI
MEMBRANE PROTEIN FOLDING AND STABILITY: Physical Principles
TL;DR: A coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins--the bilayer milieu are reviewed.
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Experimentally determined hydrophobicity scale for proteins at membrane interfaces.
TL;DR: A complete interfacial hydrophobicity scale that includes the contribution of the peptide bond was determined from the partitioning of two series of small model peptides into the interfaces of neutral (zwitterionic) phospholipid membranes.
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The Preference of Tryptophan for Membrane Interfaces
TL;DR: It is found that the interactions of four tryptophan analogues with phosphatidylcholine membranes find that the analogues reside in the vicinity of the glycerol group where they all cause similar modest changes in acyl chain organization and that hydrocarbon penetration was not increased by reduction of hydrogen bonding or electric dipole interaction ability.
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Describing the mechanism of antimicrobial peptide action with the interfacial activity model.
TL;DR: An "interfacial activity model" is proposed, which is based on an experimentally testable molecular image of AMP-membrane interactions, which may be useful in driving engineering and design of novel AMPs.
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Solvation Energies of Amino Acid Side Chains and Backbone in a Family of Host−Guest Pentapeptides
TL;DR: The very large peptide bond ASP, -96 +/- 6 cal/mol/A2, profoundly affects the results of computational comparisons of protein stability which use ASPs derived from octanol-water partitioning data.