Combining NMR relaxation with chemical shift perturbation data to drive protein-protein docking. (Q31038496)

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20 January 2020

title

Combining NMR relaxation with chemical shift perturbation data to drive protein-protein docking (English)

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20 January 2020

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3

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20 January 2020

Aalt D J van Dijk

series ordinal

1

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20 January 2020

Alexandre Bonvin

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4

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20 January 2020

author name string

Robert Kaptein

series ordinal

2

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20 January 2020

publication date

1 April 2006

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Journal of Biomolecular NMR

20 January 2020

published in

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20 January 2020

volume

34

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20 January 2020

issue

4

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20 January 2020

page(s)

237-244

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https://scigraph.springernature.com/pub.10.1007/s10858-006-0024-8

20 January 2020

exact match

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cites work

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12 December 2020

Weak alignment NMR: a hawk-eyed view of biomolecular structure

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The high-resolution structure of the histidine-containing phosphocarrier protein HPr from Escherichia coli determined by restrained molecular dynamics from nuclear magnetic resonance nuclear Overhauser effect data

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Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy

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Domain orientation in beta-cyclodextrin-loaded maltose binding protein: diffusion anisotropy measurements confirm the results of a dipolar coupling study

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Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible.

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Direct Determination of Changes of Interdomain Orientation on Ligation: Use of the Orientational Dependence of15N NMR Relaxation in Abl SH(32)†

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Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc

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Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution

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Filtering and selection of structural models: combining docking and NMR.

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Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data

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Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIAGlucose of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system

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Data-driven docking for the study of biomolecular complexes

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Principles of docking: An overview of search algorithms and a guide to scoring functions

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Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling.

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HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations.

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Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data

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The relative orientation of the fibronectin 6F1(1)F2 module pair: a 15N NMR relaxation study.

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12 December 2020

Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics.

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Identification of protein-protein interaction sites from docking energy landscapes.

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HADDOCK: a protein-protein docking approach based on biochemical or biophysical information

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12 December 2020

Principles of docking: An overview of search algorithms and a guide to scoring functions

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12 December 2020

10.1007/S10858-006-0024-8

Identifiers

DOI

1 reference

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Dimensions Publication ID

20 January 2020

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