Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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Applications of NMR and computational methodologies to study protein dynamics.Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion.Slow Dynamics of Tryptophan-Water Networks in Proteins.

P2860

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P2860

Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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2015 nî lūn-bûn

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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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Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

@ast

Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

@ast

Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

@en

P1476

Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics

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P2093

David Oyen

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

Peter E Wright

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P2860

A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments

Automated identification of functional dynamic contact networks from X-ray crystallography

Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence

The CCPN data model for NMR spectroscopy: development of a software pipeline

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Protein backbone angle restraints from searching a database for chemical shift and sequence homology

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

Binding mechanism of an SH3 domain studied by NMR and ITC.

Multiple-site exchange in proteins studied with a suite of six NMR relaxation dispersion experiments: an application to the folding of a Fyn SH3 domain mutant.

P304

5789-5798

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P31

scholarly article

P356

10.1039/C5CP04670J

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P407

English

P433

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

P478

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

P50

Robert Fenwick

P577

2016-02-01T00:00:00Z

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P698

26426424

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P932

4758882

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Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

about

P2860

P2860

Multi-probe relaxation dispersion measurements increase sensitivity to protein dynamics.

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