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A resonance assignment method for oriented-sample solid-state NMR of proteins

A resonance assignment method for oriented-sample solid-state NMR of proteins

http://www.wikidata.org/entity/Q34015910

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Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy The magic of bicelles lights up membrane protein structure NMR structures of membrane proteins in phospholipid bilayers Intrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistance Simultaneous acquisition of 2D and 3D solid-state NMR experiments for sequential assignment of oriented membrane protein samples Membrane protein structure determination: back to the membrane.On the performance of spin diffusion NMR techniques in oriented solids: prospects for resonance assignments and distance measurements from separated local field experiments.Solid state NMR strategy for characterizing native membrane protein structures Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrE A general assignment method for oriented sample (OS) solid-state NMR of proteins based on the correlation of resonances through heteronuclear dipolar couplings in samples aligned parallel and perpendicular to the magnetic field Proton evolved local field solid-state nuclear magnetic resonance using Hadamard encoding: theory and application to membrane proteins.Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins Sensitivity and resolution enhancement of oriented solid-state NMR: application to membrane proteins.Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.Covariance spectroscopy in high-resolution multi-dimensional solid-state NMR.Mechanism of dilute-spin-exchange in solid-state NMR Applications of NMR to membrane proteins.Correlating lipid bilayer fluidity with sensitivity and resolution of polytopic membrane protein spectra by solid-state NMR spectroscopy.A proton spin diffusion based solid-state NMR approach for structural studies on aligned samples.Ligand-induced conformational changes of the multidrug resistance transporter EmrE probed by oriented solid-state NMR spectroscopy.A spectroscopic assignment technique for membrane proteins reconstituted in magnetically aligned bicelles.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.Multidimensional oriented solid-state NMR experiments enable the sequential assignment of uniformly 15N labeled integral membrane proteins in magnetically aligned lipid bilayers

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P2860

A resonance assignment method for oriented-sample solid-state NMR of proteins

http://www.wikidata.org/entity/Q34015910

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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type

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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A resonance assignment method for oriented-sample solid-state NMR of proteins

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P1433

Journal of the American Chemical Society

P1476

A resonance assignment method for oriented-sample solid-state NMR of proteins

@en

P2093

Alexander A Nevzorov

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

George J Lu

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

Robert W Knox

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

Stanley J Opella

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P2860

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

Structure of the transmembrane region of the M2 protein H+ channel

Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy

Using pisa pies to resolve ambiguities in angular constraints from PISEMA spectra of aligned proteins.

Structural basis of the temperature transition of Pf1 bacteriophage

Selective averaging for high-resolution solid-state NMR spectroscopy of aligned samples.

Structure, dynamics, and assembly of filamentous bacteriophages by nuclear magnetic resonance spectroscopy.

High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR.

Structure determination of a membrane protein with two trans-membrane helices in aligned phospholipid bicelles by solid-state NMR spectroscopy.

Three-dimensional structure of the transmembrane domain of Vpu from HIV-1 in aligned phospholipid bicelles.

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8255-8257

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scholarly article

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10.1021/JA102932N

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24

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132

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2010-06-01T00:00:00Z

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44637175

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20509649

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2909040

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