A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.
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Structural basis for the slow photocycle and late proton release in Acetabularia rhodopsin I from the marine plant Acetabularia acetabulumStructure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Coordinating 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.Effect of substitution of proline-77 to aspartate on the light-driven proton release of bacteriorhodopsin.Excitation energies of a water-bridged twisted retinal structure in the bacteriorhodopsin proton pump: a theoretical investigation.
P2860
A role for internal water molecules in proton affinity changes in the Schiff base and Asp85 for one-way proton transfer in bacteriorhodopsin.
description
2008 nî lūn-bûn
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2008年の論文
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2008年論文
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2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
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2008年論文
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2008年论文
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2008年论文
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2008年论文
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name
A role for internal water mole ...... transfer in bacteriorhodopsin.
@en
type
label
A role for internal water mole ...... transfer in bacteriorhodopsin.
@en
prefLabel
A role for internal water mole ...... transfer in bacteriorhodopsin.
@en
P2093
P2860
P1476
A role for internal water mole ...... transfer in bacteriorhodopsin.
@en
P2093
Akio Maeda
Joel E Morgan
Robert B Gennis
P2860
P304
P356
10.1111/J.1751-1097.2008.00377.X
P577
2008-06-28T00:00:00Z