13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
about
NMR as a tool to investigate the structure, dynamics and function of membrane proteins.Revealing an outward-facing open conformational state in a CLC Cl(-)/H(+) exchange transporterA tale of two CLCs: biophysical insights toward understanding ClC-5 and ClC-7 function in endosomes and lysosomes.NMR studies of membrane proteins.Two Cl Ions and a Glu Compete for a Helix Cage in the CLC Proton/Cl- Antiporter.Multiscale Kinetic Modeling Reveals an Ensemble of Cl-/H+ Exchange Pathways in ClC-ec1 Antiporter.
P2860
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
description
2015 nî lūn-bûn
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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
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2015年论文
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name
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@ast
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@en
type
label
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@ast
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@en
prefLabel
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@ast
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@en
P2093
P2860
P1476
13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.
@en
P2093
Chandra M Khantwal
Corey W Liu
Merritt Maduke
Ricky C Cheng
Robert K Nakamoto
Sherwin J Abraham
Shimei Gong
Thomas A Chew
P2860
P2888
P304
P356
10.1007/S10858-015-9898-7
P577
2015-01-29T00:00:00Z