Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
about
Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfacesBuried lysine, but not arginine, titrates and alters transmembrane helix tilt.Cholesterol enhances surface water diffusion of phospholipid bilayers.Membrane-active peptides: binding, translocation, and flux in lipid vesicles.Peptides with the same composition, hydrophobicity, and hydrophobic moment bind to phospholipid bilayers with different affinities.Hydrophobic blocks facilitate lipid compatibility and translocon recognition of transmembrane protein sequencesDetermination of membrane-insertion free energies by molecular dynamics simulations.Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipidsStructurally detailed coarse-grained model for Sec-facilitated co-translational protein translocation and membrane integrationAssembly and Stability of α-Helical Membrane Proteins.Cellular crowding imposes global constraints on the chemistry and evolution of proteomes.Reconciling the roles of kinetic and thermodynamic factors in membrane-protein insertion.Functional asymmetry within the Sec61p translocon.Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.Membrane activities of colicin nuclease domains: analogies with antimicrobial peptides.Life at the border: adaptation of proteins to anisotropic membrane environment.Antibacterial surface treatment for orthopaedic implants.Plant lipid environment and membrane enzymes: the case of the plasma membrane H+-ATPase.Computational Membrane Biophysics: From Ion Channels Interactions with Drugs to Cellular Function.Phosphatidylserine Stimulates Ceramide 1-Phosphate (C1P) Intermembrane Transfer by C1P Transfer Proteins.Energetics of side-chain partitioning of β-signal residues in unassisted folding of a transmembrane β-barrel protein.Enthalpic and Entropic Contributions to HydrophobicityCharacterizing Residue-Bilayer Interactions Using Gramicidin A as a Scaffold and Tryptophan Substitutions as ProbesStructural determinants of drug partitioning in surrogates of phosphatidylcholine bilayer strataAtomistic simulations of pore formation and closure in lipid bilayers.Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.Transmembrane helices containing a charged arginine are thermodynamically stable.Insight into the interactions, residue snorkeling, and membrane disordering potency of a single antimicrobial peptide into different lipid bilayers.Refining amino acid hydrophobicity for dynamics simulation of membrane proteins.Approaches for Preparation and Biophysical Characterization of Transmembrane β-Barrels
P2860
Q30354048-4BDDE784-5072-4991-80BC-69428C4171FFQ30533993-6A5AD555-57AB-4B65-932D-DC1759E976E0Q30877135-D9CC7AFE-1EBA-418D-8AF1-7177BCD71A45Q33944833-A5271689-0D44-4F2C-885E-91DB0DD79016Q34525291-44B29D17-D4DF-44FD-A30E-7D8F4F21685DQ35551833-0238F1D0-D43E-4F46-B9CE-BF97B9B3897EQ35769994-411B2D05-DBB1-407A-BA3E-20C8B0BE2CCBQ35873948-63DB3B29-8157-439D-88DF-AE62F48E4F0EQ36318227-28333B24-BDB7-49CB-8D29-A8537D98E7BDQ36405729-7941C99E-D390-4441-A88D-C61BBBEC89D9Q36483608-1AF762FE-1AF3-4752-BB20-4E2EB28C7CD1Q36613612-E5FE7165-302C-49E1-8A1C-D926E5723392Q37340628-938C5D10-A3A8-4B4B-8D42-78198182AA67Q37406805-BEA97B99-6F3F-4191-BC47-03BA899ABE79Q38062006-304BA470-CC97-47B4-BE27-B2A87335C8E5Q38221738-3CBB1B63-53C8-452D-A4A3-E06244565775Q38239347-2E7F109A-5432-4B55-A479-1BFBDBC6F37BQ38313783-A07A0A4D-E258-42FF-BC6C-A9DA2DAAAD07Q38605343-BC70A474-BA5E-4EAA-85E9-C58EDF5F240EQ38724553-20E84363-75FC-4163-B3F0-0A201520732CQ41073405-E82E16A5-A913-4163-9DE7-D0455F28D0A3Q41099155-C45CA53F-5C81-42E9-9731-A4E016E97885Q41844419-699D2C50-ACE4-4441-84AA-AE544ED7AA3AQ41858152-E7353103-9C96-466E-93D9-F33A166A1C1EQ41900883-6B3897F6-A05C-42F6-9485-556DA817A386Q45337419-1718F3F9-335E-4B39-92FC-910EE6AEDE62Q46093219-50597F94-66FB-4ABF-9390-671B12A513FCQ47134504-76A5C473-AEDF-42B4-9930-39D0FC93CACEQ49207006-0889DBB5-8590-46CA-B92E-10DFB2C49574Q57810611-021FE7C7-C165-4E39-884C-AA173BE3E1F5
P2860
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
description
2011 nî lūn-bûn
@nan
2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@ast
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@en
type
label
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@ast
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@en
prefLabel
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@ast
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@en
P1476
Hydrophobicity scales: a thermodynamic looking glass into lipid-protein interactions.
@en
P2093
D Peter Tieleman
Justin L MacCallum
P304
P356
10.1016/J.TIBS.2011.08.003
P577
2011-09-18T00:00:00Z