Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

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Nanodiscs in Membrane Biochemistry and Biophysics.Highly Efficient Transfer of 7TM Membrane Protein from Native Membrane to Covalently Circularized Nanodisc

P2860

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P2860

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

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2015 nî lūn-bûn

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2015年の論文

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2015年学术文章

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2015年学术文章

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name

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

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Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

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type

Item

label

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

@ast

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

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prefLabel

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

@ast

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

@en

P1476

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs

@en

P2093

Jerry Chun Chung Chan

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

Julia Chuang

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

Li-Kang Chu

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

Tsung-Yen Lee

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

Tsyr-Yan Yu

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

P2860

Color Tuning in Rhodopsins: The Mechanism for the Spectral Shift between Bacteriorhodopsin and Sensory Rhodopsin II

Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins

Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane

Rhodopsin-like protein from the purple membrane of Halobacterium halobium

Proton transfer reactions in native and deionized bacteriorhodopsin upon delipidation and monomerization

The role of the native lipids and lattice structure in bacteriorhodopsin protein conformation and stability as studied by temperature-dependent Fourier transform-infrared spectroscopy.

Comparison of the dynamics of the primary events of bacteriorhodopsin in its trimeric and monomeric states.

Calcium-dependent ligand binding and G-protein signaling of family B GPCR parathyroid hormone 1 receptor purified in nanodiscs.

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.

Protein structural change at the cytoplasmic surface as the cause of cooperativity in the bacteriorhodopsin photocycle.

P304

1899-1906

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scholarly article

P356

10.1016/J.BPJ.2015.09.012

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English

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P478

109

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P50

Vivien Yeh

P577

2015-11-01T00:00:00Z

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26536266

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P932

4643209

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Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

about

P2860

P2860

Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932