Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes - Wikidata - wikimedia - TriplyDB

Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes

Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes

http://www.wikidata.org/entity/Q28833810

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Complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments.Elucidating a relationship between conformational sampling and drug resistance in HIV-1 protease.

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Quantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemes

http://www.wikidata.org/entity/Q28833810

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2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

@zh-hk

2012年論文

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2012年論文

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2012年论文

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name

Quantitative comparison of err ...... g various CPMG phasing schemes

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Quantitative comparison of err ...... g various CPMG phasing schemes

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type

label

Quantitative comparison of err ...... g various CPMG phasing schemes

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Quantitative comparison of err ...... g various CPMG phasing schemes

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prefLabel

Quantitative comparison of err ...... g various CPMG phasing schemes

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Quantitative comparison of err ...... g various CPMG phasing schemes

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Journal of Biomolecular NMR

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Quantitative comparison of err ...... g various CPMG phasing schemes

@en

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Celia A Schiffer

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

Rieko Ishima

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

Wazo Myint

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Yufeng Cai

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P2860

Crystal Structure of Lysine Sulfonamide Inhibitor Reveals the Displacement of the Conserved Flap Water Molecule in Human Immunodeficiency Virus Type 1 Protease

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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

NMR studies of protein structure and dynamics.

Dynamics of the Hck-SH3 domain: comparison of experiment with multiple molecular dynamics simulations.

Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.

Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.

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.

New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins.

Insights into the local residual entropy of proteins provided by NMR relaxation.

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s10858-012-9621-x

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13-23

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scholarly article

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10.1007/S10858-012-9621-X

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1

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4872704

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