A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data. - Wikidata - wikimedia - TriplyDB

A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data.

A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data.

http://www.wikidata.org/entity/Q34030663

about

Bioconjugation of proteins with a paramagnetic NMR and fluorescent tag.Long-range distance measurements in proteins at physiological temperatures using saturation recovery EPR spectroscopy A New Method for Determining Structure Ensemble: Application to a RNA Binding Di-Domain Protein.Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins.Visualizing transient dark states by NMR spectroscopy.Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.The double-histidine Cu²⁺-binding motif: a highly rigid, site-specific spin probe for electron spin resonance distance measurements.High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Technological advances in site-directed spin labeling of proteins.New developments in spin labels for pulsed dipolar EPR.Cu(II)-Based Paramagnetic Probe to Study RNA-Protein Interactions by NMR.Protein docking using an ensemble of spin labels optimized by intra-molecular paramagnetic relaxation enhancement.A triarylmethyl spin label for long-range distance measurement at physiological temperatures using T1 relaxation enhancement.Development of electron spin echo envelope modulation spectroscopy to probe the secondary structure of recombinant membrane proteins in a lipid bilayer.Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR.Pulsed EPR distance measurements in soluble proteins by site-directed spin labeling (SDSL).Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.Effect of a Paramagnetic Spin Label on the Intrinsically Disordered Peptide Ensemble of Amyloid-β.Yeast reveals similar molecular mechanisms underlying alpha- and beta-synuclein toxicity.

P2860

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P2860

A rigid disulfide-linked nitroxide side chain simplifies the quantitative analysis of PRE data.

http://www.wikidata.org/entity/Q34030663

description

2011 nî lūn-bûn

@nan

2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

A rigid disulfide-linked nitro ...... titative analysis of PRE data.

@ast

A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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type

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

@ast

A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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A rigid disulfide-linked nitro ...... titative analysis of PRE data.

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S10858-011-9545-X

P1433

Journal of Biomolecular NMR

P1476

A rigid disulfide-linked nitro ...... titative analysis of PRE data.

@en

P2093

G Marius Clore

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Kálmán Hideg

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

Mark R Fleissner

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

Nicholas J Anthis

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Tamás Kálai

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P2860

Linker length dependent binding of a focal adhesion kinase derived peptide to the Src SH3-SH2 domains

Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR

Structural determinants of nitroxide motion in spin-labeled proteins: Tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme

Structural origin of weakly ordered nitroxide motion in spin-labeled proteins

The Xplor-NIH NMR molecular structure determination package

Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations.

Conformational analysis of a nitroxide side chain in an α-helix with density functional theory.

Paramagnetic tagging for protein structure and dynamics analysis.

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s10858-011-9545-x

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105-114

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scholarly article

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10.1007/S10858-011-9545-X

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1-2

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51

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Nicolas L Fawzi

Wayne L. Hubbell

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2011-09-27T00:00:00Z

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51674981

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21947919

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3489005

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