Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.
about
Membrane proteins in their native habitat as seen by solid-state NMR spectroscopyProtonation of a glutamate residue modulates the dynamics of the drug transporter EmrEIntrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistanceA structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.Blocking dynamics of the SMR transporter EmrE impairs efflux activityEfficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studiesPerplexing new insight into the dynamics of the EmrE transporter.Protonation-dependent conformational dynamics of the multidrug transporter EmrE.Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Transported substrate determines exchange rate in the multidrug resistance transporter EmrE.Nuclear magnetic resonance (NMR) applied to membrane-protein complexes.Applications of NMR to membrane proteins.Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.Functional response of the small multidrug resistance protein EmrE to mutations in transmembrane helix 2.Sensitivity enhancement for membrane proteins reconstituted in parallel and perpendicular oriented bicelles obtained by using repetitive cross-polarization and membrane-incorporated free radicals.Application of paramagnetic relaxation enhancements to accelerate the acquisition of 2D and 3D solid-state NMR spectra of oriented membrane proteins.NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE.Protein Rotational Dynamics in Aligned Lipid Membranes Probed by Anisotropic T1ρ NMR Relaxation.Influence of quaternary cation compound on the size of the Escherichia coli small multidrug resistance protein, EmrE.
P2860
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P2860
Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@en
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@nl
type
label
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@en
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@nl
prefLabel
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@en
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@nl
P2093
P2860
P356
P1476
Ligand-induced conformational ...... solid-state NMR spectroscopy.
@en
P2093
Anindita Gayen
James R Banigan
Nathaniel J Traaseth
P2860
P304
10321-10324
P356
10.1002/ANIE.201303091
P407
P577
2013-08-12T00:00:00Z