Bacteriorhodopsin folds through a poorly organized transition state.
about
Kinetics of peptide folding in lipid membranesCooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops.Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease.Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability.Kinetic stability of membrane proteins.Approaches for Preparation and Biophysical Characterization of Transmembrane β-Barrels
P2860
Bacteriorhodopsin folds through a poorly organized transition state.
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Bacteriorhodopsin folds through a poorly organized transition state.
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Bacteriorhodopsin folds through a poorly organized transition state.
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label
Bacteriorhodopsin folds through a poorly organized transition state.
@en
Bacteriorhodopsin folds through a poorly organized transition state.
@nl
prefLabel
Bacteriorhodopsin folds through a poorly organized transition state.
@en
Bacteriorhodopsin folds through a poorly organized transition state.
@nl
P2093
P2860
P356
P1476
Bacteriorhodopsin folds through a poorly organized transition state.
@en
P2093
Chiwook Park
James U Bowie
Nicholas B Woodall
P2860
P304
16574-16581
P356
10.1021/JA508359N
P407
P577
2014-11-17T00:00:00Z