The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy.
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Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsinStructure of an early intermediate in the M-state phase of the bacteriorhodopsin photocycle.Maximum entropy deconvolution of infrared spectra: use of a novel entropy expression without sign restriction.Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycleControl 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 levelsThe role of small intraprotein cavities in the catalytic cycle of bacteriorhodopsin.Mapping flexible protein domains at subnanometer resolution with the atomic force microscope.Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin.Structural transition of bacteriorhodopsin is preceded by deprotonation of Schiff base: microsecond time-resolved x-ray diffraction study of purple membrane.Voltage dependence of proton pumping by bacteriorhodopsin is regulated by the voltage-sensitive ratio of M1 to M2Protein flexibility and conformational state: a comparison of collective vibrational modes of wild-type and D96N bacteriorhodopsinDynamics of different functional parts of bacteriorhodopsin: H-2H labeling and neutron scattering.Long-distance proton transfer with a break in the bacteriorhodopsin active site.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Evidence for charge-controlled conformational changes in the photocycle of bacteriorhodopsin.Thermal motions in bacteriorhodopsin at different hydration levels studied by neutron scattering: correlation with kinetics and light-induced conformational changes.Conformational change of helix G in the bacteriorhodopsin photocycle: investigation with heavy atom labeling and x-ray diffraction.Time-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.Time-resolved detection of transient movement of helices F and G in doubly spin-labeled bacteriorhodopsin.Can the low-resolution structures of photointermediates of bacteriorhodopsin explain their crystal structures?Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography.Spin-labeling studies of the conformational changes in the vicinity of D36, D38, T46, and E161 of bacteriorhodopsin during the photocycleTwo forms of N intermediate (N(open) and N(closed)) in the bacteriorhodopsin photocycle.Subdomains in the F and G helices of bacteriorhodopsin regulate the conformational transitions of the reprotonation mechanism.Structural differences between the closed and open states of channelrhodopsin-2 as observed by EPR spectroscopy.
P2860
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P2860
The tertiary structural changes in bacteriorhodopsin occur between M states: X-ray diffraction and Fourier transform infrared spectroscopy.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
The tertiary structural change ...... ansform infrared spectroscopy.
@en
The tertiary structural change ...... ansform infrared spectroscopy.
@nl
type
label
The tertiary structural change ...... ansform infrared spectroscopy.
@en
The tertiary structural change ...... ansform infrared spectroscopy.
@nl
prefLabel
The tertiary structural change ...... ansform infrared spectroscopy.
@en
The tertiary structural change ...... ansform infrared spectroscopy.
@nl
P2093
P2860
P356
P1433
P1476
The tertiary structural change ...... ansform infrared spectroscopy.
@en
P2093
Dencher NA
Oesterhelt D
Schachowa IW
P2860
P304
P356
10.1093/EMBOJ/16.7.1484
P407
P577
1997-04-01T00:00:00Z