Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates.
about
Energy transduction: proton transfer through the respiratory complexesFTIR spectroscopy of the M photointermediate in pharaonis rhoborhodopsin.Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycleFourier transform infrared spectroscopic analysis of altered reaction pathways in site-directed mutants: the D212N mutant of bacteriorhodopsin expressed in Halobacterium halobium.A large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins.The effect of protein conformation change from alpha(II) to alpha(I) on the bacteriorhodopsin photocycle.The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species.Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycleMolecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.Guanidinium restores the chromophore but not rapid proton release in bacteriorhodopsin mutant R82QNanosecond retinal structure changes in K-590 during the room-temperature bacteriorhodopsin photocycle: picosecond time-resolved coherent anti-stokes Raman spectroscopyReorientations in the bacteriorhodopsin photoscycle are pH dependent.Two progressive substrates of the M-intermediate can be identified in glucose-embedded, wild-type bacteriorhodopsin.pH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopyLight-induced reorientation in the purple membrane.Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsinMolecular dynamics study of the M412 intermediate of bacteriorhodopsin.Photochemical reaction cycle and proton transfers in Neurospora rhodopsin.Further studies with isolated absolute infrared spectra of bacteriorhodopsin photocycle intermediates: conformational changes and possible role of a new proton-binding center.Connectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access modelInfrared and visible absolute and difference spectra of bacteriorhodopsin photocycle intermediates.Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle.Conformational changes in the archaerhodopsin-3 proton pump: detection of conserved strongly hydrogen bonded water networksWater as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin.Structural and energetic determinants of primary proton transfer in bacteriorhodopsin.A local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin.Reversible steps in the bacteriorhodopsin photocycle.Photocycle of Exiguobacterium sibiricum rhodopsin characterized by low-temperature trapping in the IR and time-resolved studies in the visibleMechanism divergence in microbial rhodopsins.The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates.Replacement of leucine-93 by alanine or threonine slows down the decay of the N and O intermediates in the photocycle of bacteriorhodopsin: implications for proton uptake and 13-cis-retinal----all-trans-retinal reisomerization.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.Fibroblast growth factor receptors participate in the control of mitogen-activated protein kinase activity during nerve growth factor-induced neuronal differentiation of PC12 cells.Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy.Functional interactions in bacteriorhodopsin: a theoretical analysis of retinal hydrogen bonding with water.A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.Evidence for charge-controlled conformational changes in the photocycle of bacteriorhodopsin.Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics.The structures of bacteriorhodopsin with different retinal-Schiff base orientations--computer modeling and energy minimization studies.
P2860
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P2860
Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates.
description
1991 nî lūn-bûn
@nan
1991 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի մարտին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Protein dynamics in the bacter ...... , M, and N photointermediates.
@ast
Protein dynamics in the bacter ...... , M, and N photointermediates.
@en
type
label
Protein dynamics in the bacter ...... , M, and N photointermediates.
@ast
Protein dynamics in the bacter ...... , M, and N photointermediates.
@en
prefLabel
Protein dynamics in the bacter ...... , M, and N photointermediates.
@ast
Protein dynamics in the bacter ...... , M, and N photointermediates.
@en
P2093
P2860
P356
P1476
Protein dynamics in the bacter ...... , M, and N photointermediates.
@en
P2093
K J Rothschild
M S Braiman
P2860
P304
P356
10.1073/PNAS.88.6.2388
P407
P577
1991-03-01T00:00:00Z