The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species.
about
Filming biomolecular processes by high-speed atomic force microscopyHigh-field EPR spectroscopy applied to biological systems: characterization of molecular switches for electron and ion transfer.Structural transition of bacteriorhodopsin is preceded by deprotonation of Schiff base: microsecond time-resolved x-ray diffraction study of purple membrane.Thermal equilibration between the M and N intermediates in the photocycle of bacteriorhodopsinFunctional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle.Molecular dynamics study of the M412 intermediate of bacteriorhodopsin.Rapid pH change due to bacteriorhodopsin measured with a tin-oxide electrode.Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access modelMicrosecond atomic force sensing of protein conformational dynamics: implications for the primary light-induced events in bacteriorhodopsinDirectly probing rapid membrane protein dynamics with an atomic force microscope: a study of light-induced conformational alterations in bacteriorhodopsinTime-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin.Unraveling photoexcited conformational changes of bacteriorhodopsin by time resolved electron paramagnetic resonance spectroscopy.The M intermediate of Pharaonis phoborhodopsin is photoactive.Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin.Fourier transform infrared double-flash experiments resolve bacteriorhodopsin's M1 to M2 transition.A model-independent approach to assigning bacteriorhodopsin's intramolecular reactions to photocycle intermediates.Two forms of N intermediate (N(open) and N(closed)) in the bacteriorhodopsin photocycle.Evidence for the first phase of the reprotonation switch of bacteriorhodopsin from time-resolved photovoltage and flash photolysis experiments on the photoreversal of the M-intermediate.The pH dependence of the subpicosecond retinal photoisomerization process in bacteriorhodopsin: evidence for parallel photocycles.Transition of rhodopsin into the active metarhodopsin II state opens a new light-induced pathway linked to Schiff base isomerization.Inhibition of the M1-->M2 (M(closed) --> M(open)) transition in the D96N mutant photocycle and its relation to the corresponding transition in wild-type bacteriorhodopsin.
P2860
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P2860
The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species.
description
1992 nî lūn-bûn
@nan
1992 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
The back photoreaction of the ...... nd evidence for two M species.
@ast
The back photoreaction of the ...... nd evidence for two M species.
@en
type
label
The back photoreaction of the ...... nd evidence for two M species.
@ast
The back photoreaction of the ...... nd evidence for two M species.
@en
prefLabel
The back photoreaction of the ...... nd evidence for two M species.
@ast
The back photoreaction of the ...... nd evidence for two M species.
@en
P2093
P2860
P1476
The back photoreaction of the ...... nd evidence for two M species.
@en
P2093
M Ottolenghi
N Friedman
R Needleman
S Druckmann
P2860
P304
P356
10.1111/J.1751-1097.1992.TB09727.X
P577
1992-01-01T00:00:00Z