Parameterization of Peptide13C Carbonyl Chemical Shielding Anisotropy in Molecular Dynamics Simulations (Q57828531)

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31 December 2019

title

Parameterization of peptide 13C carbonyl chemical shielding anisotropy in molecular dynamics simulations (English)

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1

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31 December 2019

Maria Mills

2

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31 December 2019

author name string

Ioan Andricioaei

3

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31 December 2019

Akash Bhattacharya

4

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Kim Palmo

5

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31 December 2019

Erik R P Zuiderweg

6

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publication date

1 June 2007

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31 December 2019

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volume

8

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issue

9

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page(s)

1375-1385

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All-atom empirical potential for molecular modeling and dynamics studies of proteins

31 December 2019

cites work

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Backbone Dynamics of the Ribonuclease Binase Active Site Area Using Multinuclear (15N and13CO) NMR Relaxation and Computational Molecular Dynamics†

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Changes in calmodulin main-chain dynamics upon ligand binding revealed by cross-correlated NMR relaxation measurements

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Site-Specific Variations of Carbonyl Chemical Shift Anisotropies in Proteins

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Chemical shift anisotropy tensors of carbonyl, nitrogen, and amide proton nuclei in proteins through cross-correlated relaxation in NMR spectroscopy

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Determination of chemical shift anisotropy tensors of carbonyl nuclei in proteins through cross-correlated relaxation in NMR

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Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy

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7 January 2021

Temperature dependence of protein backbone motion from carbonyl 13C and amide 15N NMR relaxation

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Quantifying Lipari-Szabo modelfree parameters from 13CO NMR relaxation experiments

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Probing multiple effects on 15N, 13C alpha, 13C beta, and 13C' chemical shifts in peptides using density functional theory

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Identifiers

DOI

10.1002/CPHC.200700003

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31 December 2019

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