Water: foldase activity in catalyzing polypeptide conformational rearrangements
about
Structure of the transmembrane region of the M2 protein H+ channelBackbone structure of a small helical integral membrane protein: A unique structural characterizationSolid state NMR: The essential technology for helical membrane protein structural characterization.Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Water lubricates hydrogen-bonded molecular machines.Uniformity, ideality, and hydrogen bonds in transmembrane alpha-helices.Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Probing Residue-Specific Water-Protein Interactions in Oriented Lipid Membranes via Solid-State NMR Spectroscopy.Differences in the transactivation domains of p53 family members: a computational study.Mass spectrometry of proteins of known massStructural restraints and heterogeneous orientation of the gramicidin A channel closed state in lipid bilayers.Large scale conformational transitions in β-structural motif of gramicidin A: kinetic analysis based on CD and FT-IR data.Transmembrane helix uniformity examined by spectral mapping of torsion angles.Influences of membrane mimetic environments on membrane protein structures.Helical membrane protein conformations and their environmentSensing Tryptophan Microenvironment of Amyloid Protein Utilizing Wavelength-Selective Fluorescence Approach.Effect of graded hydration on the dynamics of an ion channel peptide: a fluorescence approach.Hierarchical structure of the energy landscape of proteins revisited by time series analysis. II. Investigation of explicit solvent effects.Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.Protein folding kinetics and thermodynamics from atomistic simulations.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
P2860
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P2860
Water: foldase activity in catalyzing polypeptide conformational rearrangements
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@ast
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@en
type
label
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@ast
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@en
prefLabel
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@ast
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@en
P2860
P356
P1476
Water: foldase activity in catalyzing polypeptide conformational rearrangements
@en
P2860
P304
P356
10.1073/PNAS.96.16.9057
P407
P577
1999-08-01T00:00:00Z