title: Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
abstract: The partitioning of amino acid sidechains into the membrane is a key aspect of membrane protein folding. However, lipid bilayers exhibit rapidly changing physicochemical properties over their nanometer-scale thickness, which complicates understanding the thermodynamics and microscopic details of membrane partitioning. Recent data from diverse approaches, including protein insertion by the Sec translocon, folding of a small beta-barrel membrane protein and computer simulations of the exact distribution of a variety of small molecules and peptides, have joined older hydrophobicity scales for membrane protein prediction. We examine the correlations among the scales and find that they are remarkably correlated even though there are large differences in magnitude. We discuss the implications of these scales for understanding membrane protein structure and function.
authors.affiliation: Laufer Center for Physical and Quantitative Biology, Stony Brook University, Stony Brook, NY 11794, USA. justin.maccallum@me.com
authors.forename: Justin L
authors.initials: JL
authors.lastname: MacCallum
authors.forename: D Peter
authors.initials: DP
authors.lastname: Tieleman
mesh_terms: D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008055:Lipids / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008055:Lipids; D008565:Membrane Proteins