Stephen H. White

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.

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.

TL;DR: A comprehensive classification of lipids with a common platform that is compatible with informatics requirements has been developed to deal with the massive amounts of data that will be generated by the lipid community.

TL;DR: The results indicate that direct protein–lipid interactions are critical during translocon-mediated membrane insertion, and the basic features of this code are determined, including a ‘biological’ hydrophobicity scale.

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.