Contribution of proton release to the B2 photocurrent of bacteriorhodopsin - Wikidata - wikimedia - TriplyDB

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

http://www.wikidata.org/entity/Q34168433

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Time-resolved rhodopsin activation currents in a unicellular expression system.Normal and mutant rhodopsin activation measured with the early receptor current in a unicellular expression system.

P2860

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P2860

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

http://www.wikidata.org/entity/Q34168433

description

1998 nî lūn-bûn

@nan

1998 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

name

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@ast

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@en

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@nl

type

label

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@ast

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@en

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@nl

prefLabel

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@ast

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@en

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@nl

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P356

S0006-3495(98)77522-8

P1433

Biophysical Journal

P1476

Contribution of proton release to the B2 photocurrent of bacteriorhodopsin

@en

P2093

S Misra

http://www.w3.org/2001/XMLSchema#string

P2860

X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases

Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsin.

Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it

Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.

Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.

Effect of pH buffer molecules on the light-induced currents from oriented purple membrane.

Light-induced currents from oriented purple membrane: I. Correlation of the microsecond component (B2) with the L-M photocycle transition.

Light-induced currents from oriented purple membrane: II. Proton and cation contributions to the photocurrent

Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle

P304

382-388

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P31

scholarly article

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10.1016/S0006-3495(98)77522-8

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P433

1

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75

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1998-07-01T00:00:00Z

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13636169

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9649395

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1299707

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