The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.
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Bioenergetics of the Archaea.Photocycle of dried acid purple form of bacteriorhodopsinFactors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Time-resolved Fourier transform infrared spectroscopy of the polarizable proton continua and the proton pump mechanism of bacteriorhodopsinA natural light-driven inward proton pump.The protonation-deprotonation kinetics of the protonated Schiff base in bicelle bacteriorhodopsin crystalsPhotochromicity of Anabaena sensory rhodopsin, an atypical microbial receptor with a cis-retinal light-adapted form.pH (low) insertion peptide (pHLIP) inserts across a lipid bilayer as a helix and exits by a different path.Guanidinium restores the chromophore but not rapid proton release in bacteriorhodopsin mutant R82QPhotoproducts of bacteriorhodopsin mutants: a molecular dynamics study.Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores itArginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsinEvidence that aspartate-85 has a higher pK(a) in all-trans than in 13-cisbacteriorhodopsin.Perturbed interaction between residues 85 and 204 in Tyr-185-->Phe and Asp-85-->Glu bacteriorhodopsins.Nature of the chromophore binding site of bacteriorhodopsin: the potential role of Arg82 as a principal counterion.Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin.On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsinMolecular dynamics study of the nature and origin of retinal's twisted structure in bacteriorhodopsin.Characterization of the proton-transporting photocycle of pharaonis halorhodopsinpH dependence of light-driven proton pumping by an archaerhodopsin from Tibet: comparison with bacteriorhodopsin.Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle.Identification of Specific Effect of Chloride on the Spectral Properties and Structural Stability of Multiple Extracellular Glutamic Acid Mutants of Bacteriorhodopsin.Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Long-distance proton transfer with a break in the bacteriorhodopsin active site.Molecular basis for pH sensitivity and proton transfer in green fluorescent protein: protonation and conformational substates from electrostatic calculationsCoordinating the structural rearrangements associated with unidirectional proton transfer in the bacteriorhodopsin photocycle induced by deprotonation of the proton-release group: a time-resolved difference FTIR spectroscopic study.Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy.Simulation analysis of the retinal conformational equilibrium in dark-adapted bacteriorhodopsin.Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin.Conformational changes of bacteriorhodopsin along the proton-conduction chain as studied with (13)C NMR of [3-(13)C]Ala-labeled protein: arg(82) may function as an information mediator.Fourier transform infrared evidence for early deprotonation of Asp(85) at alkaline pH in the photocycle of bacteriorhodopsin mutants containing E194Q.Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II).Role of Arg-72 of pharaonis Phoborhodopsin (sensory rhodopsin II) on its photochemistry.Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps.Titration of aspartate-85 in bacteriorhodopsin: what it says about chromophore isomerization and proton release.Factors that differentiate the H-bond strengths of water near the Schiff bases in bacteriorhodopsin and Anabaena sensory rhodopsin.Shuffling protons in bacteriorhodopsin: long-distance coupling between the pKas of two carboxylic groups.pH-dependent transitions in xanthorhodopsin.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.
P2860
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P2860
The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
The two pKa's of aspartate-85 ...... e mutant of bacteriorhodopsin.
@en
type
label
The two pKa's of aspartate-85 ...... e mutant of bacteriorhodopsin.
@en
prefLabel
The two pKa's of aspartate-85 ...... e mutant of bacteriorhodopsin.
@en
P2093
P356
P1433
P1476
The two pKa's of aspartate-85 ...... ne mutant of bacteriorhodopsin
@en
P2093
D R Menick
E S Imasheva
R Govindjee
R K Crouch
S P Balashov
P304
P356
10.1021/BI00027A034
P407
P50
P577
1995-07-01T00:00:00Z