期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1828, 期 2, 页码 864-876出版社
ELSEVIER
DOI: 10.1016/j.bbamem.2012.09.009
关键词
Protein-lipid interactions; Tryptophan; Membrane protein; Hydrophobic mismatch; Molecular Dynamics; Free energy
资金
- National Science Foundation [MCB-1052477]
- Australian Research Council [DP120103548]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1052477] Funding Source: National Science Foundation
Tryptophan (Trp) is abundant in membrane proteins, preferentially residing near the lipid-water interface where it is thought to play a significant anchoring role. Using a total of 3 mu s of molecular dynamics simulations for a library of hydrophobic WALP-like peptides, a long poly-Leu alpha-helix, and the methyl-indole analog, we explore the thermodynamics of the Trp movement in membranes that governs the stability and orientation of transmembrane protein segments. We examine the dominant hydrogen-bonding interactions between the Trp and lipid carbonyl and phosphate moieties, cation-pi interactions to lipid choline moieties, and elucidate the contributions to the thermodynamics that serve to localize the Trp, by similar to 4 kcal/mol, near the membrane glycerol backbone region. We show a striking similarity between the free energy to move an isolated Trp side chain to that found from a wide range of WALP peptides, suggesting that the location of this side chain is nearly independent of the host transmembrane segment. Our calculations provide quantitative measures that explain Trp's role as a modulator of responses to hydrophobic mismatch, providing a deeper understanding of how lipid composition may control a range of membrane active peptides and proteins. Published by Elsevier B.V.
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