Energetics of hydrophobic matching in lipid-protein interactions.
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Summary
Segmental order parameters confirm that elastic lipid chain distortions are insufficient to compensate fully for the mismatch, but the dependence on chain length with tryptophan-anchored peptides requires that the free energy density of hydrophobic mismatch should increase with increasing extent of mismatch.
- Type
- article
- Published
- 2008-05-15
- Cited by
- 113
- References
- 94
- OpenAlex
- https://openalex.org/W18234817
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:28404443
Keywords
Psychology, Social psychology, Epistemology, Philosophy
References
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- Lateral pressure in membranes.
- Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid.
- A molecular model for lipid-protein interaction in membranes: the role of hydrophobic mismatch.
Cited by
- Canonical azimuthal rotations and flanking residues constrain the orientation of transmembrane helices.
- How the dynamic properties and functional mechanisms of GPCRs are modulated by their coupling to the membrane environment.
- Why GPCRs behave differently in cubic and lamellar lipidic mesophases
- Design, synthesis and study of the biological and biophysical activity of antimicrobial peptides
- Pushing the boundaries : molecular dynamics simulations of complex biological membranes
- Computational studies of the interactions of biologically active peptides with membrane
- Assessment of the Functionality and Stability of Detergent Purified nAChR from Torpedo using Lipidic Matrixes and Macroscopic Electrophysiology
- Lipid-protein interactions.
- Hydrophobic Mismatch Drives the Interaction of E5 with the Transmembrane Segment of PDGF Receptor
- Regulation of Aquaporin Z osmotic permeability in ABA tri-block copolymer
- Life at the border: Adaptation of proteins to anisotropic membrane environment
- Monte Carlo simulations of peptide–membrane interactions with the MCPep web server
- Helical Membrane Protein Conformations and their Environment
- Lipid shape is a key factor for membrane interactions of amphipathic helical peptides.
- Orientation and conformation of lipids in crystals of transmembrane proteins
- Structural and thermodynamic determinants of chain-melting transition temperatures for phospholipid and glycolipids membranes.
- Effect of integral proteins in the phase stability of a lipid bilayer: application to raft formation in cell membranes.
- Synergistic insertion of antimicrobial magainin-family peptides in membranes depends on the lipid spontaneous curvature.
- Structural biology: Highly charged meetings
- Intramembrane water associated with TOAC spin-labeled alamethicin: electron spin-echo envelope modulation by D2O.
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