Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins
about
Lessons from the lysozyme of phage T4The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.Fragment-based phase extension for three-dimensional structure determination of membrane proteins by electron crystallography.Stable folding core in the folding transition state of an alpha-helical integral membrane protein.Interactions between ionizable amino acid side chains at a lipid bilayer-water interface.Constructing and validating initial Cα models from subnanometer resolution density maps with pathwalkingMarginally hydrophobic transmembrane α-helices shaping membrane protein folding.Forces stabilizing proteinsThe safety dance: biophysics of membrane protein folding and misfolding in a cellular contextViroporins, Examples of the Two-Stage Membrane Protein Folding Model.Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Reversible folding of human peripheral myelin protein 22, a tetraspan membrane protein.Architectural and thermodynamic principles underlying intramembrane protease function.Thermodynamic stability of bacteriorhodopsin mutants measured relative to the bacterioopsin unfolded state.Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability.Contribution of hydrophobic interactions to protein stability.Knowledge-based potential for positioning membrane-associated structures and assessing residue-specific energetic contributionsStructural differences between thermophilic and mesophilic membrane proteins.Comparison of NMR and crystal structures of membrane proteins and computational refinement to improve model quality.Multi-spectroscopic and theoretical analyses on the diphenyl ether-tert-butyl alcohol complex in the electronic ground and electronically excited state.The Structure of Diphenyl Ether-Methanol in the Electronically Excited and Ionic Ground States: A Combined IR/UV Spectroscopic and Theoretical Study.Ultra light-sensitive and fast neuronal activation with the Ca²+-permeable channelrhodopsin CatCh.Comparing side chain packing in soluble proteins, protein-protein interfaces, and transmembrane proteins.Steric interactions determine side-chain conformations in protein cores.Tuning the coordination chemistry of cyclotriveratrylene ligand pairs through alkyl chain aggregation
P2860
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P2860
Similar Energetic Contributions of Packing in the Core of Membrane and Water-Soluble Proteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@ast
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@en
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@nl
type
label
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@ast
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@en
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@nl
prefLabel
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@ast
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@en
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@nl
P2093
P2860
P356
P1476
Similar Energetic Contribution ...... ane and Water-Soluble Proteins
@en
P2093
Amit Oberai
James U Bowie
Nathan H Joh
P2860
P304
P356
10.1021/JA904711K
P407
P577
2009-08-12T00:00:00Z