Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.
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Bioenergetics of the Archaea.Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsinMolecular mechanism of vectorial proton translocation by bacteriorhodopsinStructure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle.Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsinFTIR spectroscopy of the M photointermediate in pharaonis rhoborhodopsin.High-field EPR spectroscopy applied to biological systems: characterization of molecular switches for electron and ion transfer.The bacteriorhodopsin photocycle: direct structural study of two substrates of the M-intermediate.Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycleStructural changes in the L photointermediate of bacteriorhodopsin.The effect of protein conformation change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle.Control of the pump cycle in bacteriorhodopsin: mechanisms elucidated by solid-state NMR of the D85N mutant.Deuterium solid-state NMR investigations of exchange labeled oriented purple membranes at different hydration levelsProtein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses.The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy.Time-resolved long-lived infrared emission from bacteriorhodopsin during its photocycle.Mapping flexible protein domains at subnanometer resolution with the atomic force microscope.Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycleProgress toward an explicit mechanistic model for the light-driven pump, bacteriorhodopsin.His166 is critical for active-site proton transfer and phototaxis signaling by sensory rhodopsin I.Chromophore reorientations in the early photolysis intermediates of bacteriorhodopsin.Reorientations in the bacteriorhodopsin photoscycle are pH dependent.Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin.Light-induced reorientation in the purple membrane.Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.A residue substitution near the beta-ionone ring of the retinal affects the M substates of bacteriorhodopsinWhat spectroscopy can still tell us about the secondary structure of bacteriorhodopsinProtein flexibility and conformational state: a comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsinReversible monolayer-to-crystalline phase transition in amphiphilic silsesquioxane at the air-water interface.Proton transfer via a transient linear water-molecule chain in a membrane protein.Effect of cytosolic pH on inward currents reveals structural characteristics of the proton transport cycle in the influenza A protein M2 in cell-free membrane patches of Xenopus oocytesX-ray diffraction of bacteriorhodopsin photocycle intermediates.Time-resolved x-ray diffraction reveals multiple conformations in the M-N transition of the bacteriorhodopsin photocycleLight-induced isomerization causes an increase in the chromophore tilt in the M intermediate of bacteriorhodopsin: a neutron diffraction study.Electron diffraction studies of light-induced conformational changes in the Leu-93 --> Ala bacteriorhodopsin mutant.Dynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering.Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductanceIn situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopyThermal motions and function of bacteriorhodopsin in purple membranes: effects of temperature and hydration studied by neutron scatteringA local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin.
P2860
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P2860
Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.
description
1989 nî lūn-bûn
@nan
1989 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Structural changes in bacterio ...... vealed by neutron diffraction.
@ast
Structural changes in bacterio ...... vealed by neutron diffraction.
@en
Structural changes in bacterio ...... vealed by neutron diffraction.
@nl
type
label
Structural changes in bacterio ...... vealed by neutron diffraction.
@ast
Structural changes in bacterio ...... vealed by neutron diffraction.
@en
Structural changes in bacterio ...... vealed by neutron diffraction.
@nl
prefLabel
Structural changes in bacterio ...... vealed by neutron diffraction.
@ast
Structural changes in bacterio ...... vealed by neutron diffraction.
@en
Structural changes in bacterio ...... vealed by neutron diffraction.
@nl
P2093
P2860
P356
P1476
Structural changes in bacterio ...... vealed by neutron diffraction.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.20.7876
P407
P577
1989-10-01T00:00:00Z