Conformational changes in bacteriorhodopsin associated with protein-protein interactions: a functional .alpha.I-.alpha.II helix switch?
about
The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy.In-Situ Observation of Membrane Protein Folding during Cell-Free ExpressionA (13)C NMR study on [3-(13)C]-, [1-(13)C]Ala-, or [1-(13)C]Val-labeled transmembrane peptides of bacteriorhodopsin in lipid bilayers: insertion, rigid-body motions, and local conformational fluctuations at ambient temperature.Structure of the influenza C virus CM2 protein transmembrane domain obtained by site-specific infrared dichroism and global molecular dynamics searching.
P2860
Conformational changes in bacteriorhodopsin associated with protein-protein interactions: a functional .alpha.I-.alpha.II helix switch?
description
im Dezember 1995 veröffentlicher wissenschaftlicher Artikel
@de
scientific article published on 01 December 1995
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в грудні 1995
@uk
name
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@en
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@nl
type
label
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@en
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@nl
prefLabel
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@en
Conformational changes in bact ...... lpha.I-.alpha.II helix switch?
@nl
P356
P1433
P1476
Conformational changes in bact ...... alpha I-alpha II helix switch?
@en
P2093
P304
16320-16326
P356
10.1021/BI00050A012
P407
P577
1995-12-01T00:00:00Z