[NMR paper] Anisotropic Dynamics of Protein Side Chain NH(2) Groups Revealed through Analysis of (2)H and (15)N NMR Relaxation Rates
Anisotropic Dynamics of Protein Side Chain NH(2) Groups Revealed through Analysis of (2)H and (15)N NMR Relaxation Rates
Although nuclear magnetic resonance (NMR) spectroscopy is powerful for protein dynamics investigations, the anisotropy of internal motions has been difficult to analyze with NMR. In principle, NMR order parameters for multiple bond vectors fixed on the same plane can reveal the anisotropy of internal motions. We investigated the anisotropic dynamics of protein asparagine (Asn) and glutamine (Gln) side chain NH(2) groups using ²H and ^(15)N NMR relaxation rates. Hindered...
Basic Experiments in 2H static NMR for the Characterization of Protein Side-Chain Dynamics
Basic Experiments in 2H static NMR for the Characterization of Protein Side-Chain Dynamics
Publication date: Available online 27 April 2018
Source:Methods</br>
Author(s): Liliya Vugmeyster, Dmitry Ostrovsky</br>
The focus of this review is the basic methodology for applications of static deuteron NMR for studies of dynamics in the side chains of proteins. We review experimental approaches for the measurements of static line shapes and relaxation rates as well as signal enhancement strategies using the multiple echo acquisition scheme. Further, we describe...
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Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Probing Protein Side Chain Dynamics via (13)C NMR Relaxation.
Protein Pept Lett. 2011 Jan 11;
Authors: Yang D
Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, (13)C relaxation of methine, methylene and methyl groups with and without...
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01-13-2011 12:00 PM
[NMR paper] What contributions to protein side-chain dynamics are probed by NMR experiments? A mo
What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
Related Articles What contributions to protein side-chain dynamics are probed by NMR experiments? A molecular dynamics simulation analysis.
J Mol Biol. 2005 May 27;349(1):185-203
Authors: Best RB, Clarke J, Karplus M
Molecular dynamics simulations of the structurally homologous proteins TNfn3 and FNfn10 have been used to investigate the contributions to side-chain dynamics measured by NMR relaxation experiments. The...
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11-24-2010 11:14 PM
[NMR paper] Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studi
Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Related Articles Main chain and side chain dynamics of a heme protein: 15N and 2H NMR relaxation studies of R. capsulatus ferrocytochrome c2.
Biochemistry. 2001 Jun 5;40(22):6559-69
Authors: Flynn PF, Bieber Urbauer RJ, Zhang H, Lee AL, Wand AJ
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is...
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11-19-2010 08:32 PM
[NMR paper] A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-cor
A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
Related Articles A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk.
J Mol Biol. 1998 Mar 13;276(5):939-54
Authors: Yang D, Mittermaier A, Mok YK, Kay LE
Two new NMR experiments are presented for measuring side-chain dynamics in proteins. The first method, requiring 15N, 13C,...
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11-17-2010 11:06 PM
[NMR paper] A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
Related Articles A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
J Magn Reson. 1998 Feb;130(2):329-34
Authors: Daragan VA, Mayo KH
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational...
Anisotropic Dynamics of Protein Side Chain NH - ACS Publications
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