The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.
about
Methionine changes in bacteriorhodopsin detected by FTIR and cell-free selenomethionine substitutionGlutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin.Structural characterization of the L-to-M transition of the bacteriorhodopsin photocycleStructural changes in the L photointermediate of bacteriorhodopsin.Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses.Molecular mechanism of protein-retinal coupling in bacteriorhodopsin.Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycleConnectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access modelWater 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.Structural changes in the N and N' states of the bacteriorhodopsin photocycleA role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.Long-distance effects of site-directed mutations on backbone conformation in bacteriorhodopsin from solid state NMR of [1-13C]Val-labeled proteins.Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR.Mechanism of ion transport across membranes. Bacteriorhodopsin as a prototype for proton pumps.Molecular details of the unique mechanism of chloride transport by a cyanobacterial rhodopsin.Mutation of arginine 134 to lysine alters the pK(a)s of key groups involved in proton pumping by bacteriorhodopsin.
P2860
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P2860
The retinal Schiff base-counterion complex of bacteriorhodopsin: changed geometry during the photocycle is a cause of proton transfer to aspartate 85.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
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1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
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1994年學術文章
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1994年學術文章
@zh-hant
name
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@en
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@nl
type
label
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@en
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@nl
prefLabel
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@en
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@nl
P2093
P356
P1433
P1476
The retinal Schiff base-counte ...... oton transfer to aspartate 85.
@en
P2093
Needleman R
Yamazaki Y
P304
12001-12011
P356
10.1021/BI00206A001
P407
P577
1994-10-01T00:00:00Z