(Q30328450)

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Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy.

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Europe PubMed Central

18 June 2017

Nuclear magnetic resonance relaxation in determination of residue-specific 15N chemical shift tensors in proteins in solution: protein dynamics, structure, and applications of transverse relaxation optimized spectroscopy. (English)

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Europe PubMed Central

18 June 2017

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Fushman D

1

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18 June 2017

Cowburn D

2

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18 June 2017

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publication date

1 January 2001

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18 June 2017

Methods in Enzymology

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18 June 2017

339

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18 June 2017

109-126

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Europe PubMed Central

18 June 2017

Chemical shifts as a tool for structure determination

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Chemical shifts and three-dimensional protein structures

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Orientational constraints as three-dimensional structural constraints from chemical shift anisotropy: the polypeptide backbone of gramicidin A in a lipid bilayer

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Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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The effect of noncollinearity of 15N-1H dipolar and 15N CSA tensors and rotational anisotropy on 15N relaxation, CSA/dipolar cross correlation, and TROSY.

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Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

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Protein Backbone Dynamics and 15 N Chemical Shift Anisotropy from Quantitative Measurement of Relaxation Interference Effects

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Quantitative estimation of magnitude and orientation of the CSA tensor from field dependence of longitudinal NMR relaxation rates

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Protein backbone dynamics revealed by quasi spectral density function analysis of amide N-15 nuclei

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Spectral density function mapping using 15N relaxation data exclusively

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Direct Measurement of15N Chemical Shift Anisotropy in Solution

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Model-Independent Analysis of15N Chemical Shift Anisotropy from NMR Relaxation Data. Ubiquitin as a Test Example

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The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration 1 1 Edited by P.E.Wright

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An Approach to Direct Determination of Protein Dynamics from15N NMR Relaxation at Multiple Fields, Independent of Variable15N Chemical Shift Anisotropy and Chemical Exchange Contributions

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Backbone dynamics of ribonuclease T1 and its complex with 2'GMP studied by two-dimensional heteronuclear NMR spectroscopy

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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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Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins

1 reference

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Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13C alpha nuclear spin relaxation

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Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure

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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

1 reference

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Sequence-Corrected 15N "Random Coil" Chemical Shifts

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Identifiers

10.1016/S0076-6879(01)39312-6

1 reference

Europe PubMed Central

18 June 2017

1 reference

Europe PubMed Central

18 June 2017

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