Amino-acid side-chain properties in proteins are key determinants of protein function. NMR spin relaxation of side chains is an important source of information about local protein dynamics and flexibility. However, traditional solution NMR relaxation methods are most sensitive to sub-nanosecond dynamics lacking information on slower ns-?s time-scale motions. Nanoparticle-assisted NMR spin relaxation (NASR) of methyl-side chains is introduced here as a window into these ns-?s dynamics. NASR...
[ASAP] Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation
Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation
Xinyao Xiang, Alexandar L. Hansen, Lei Yu, Gregory Jameson, Lei Bruschweiler-Li, Chunhua Yuan, and Rafael Bru?schweiler
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.1c04687/20210824/images/medium/ja1c04687_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.1c04687
http://feeds.feedburner.com/~r/acs/jacsat/~4/8joQZH1-cyY
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[NMR paper] Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups
Probing Side-Chain Dynamics in Proteins by NMR Relaxation of Isolated (13)C Magnetization Modes in (13)CH(3) Methyl Groups
The dynamics of methyl-bearing side chains in proteins were probed by ^(13)C relaxation measurements of a number of ^(13)C magnetization modes in selectively ^(13)CH(3)-labeled methyl groups of proteins. We first show how ^(13)C magnetization modes in a ^(13)CH(3) spin-system can be isolated using acute-angle ¹H radio-frequency pulses. The parameters of methyl-axis dynamics, a measure of methyl-axis ordering (S(axis)²) and the correlation time of fast local methyl-axis...
[NMR paper] Broadband Dynamics of Ubiquitin by Anionic and Cationic Nanoparticle-Assisted NMR Spin Relaxation.
Broadband Dynamics of Ubiquitin by Anionic and Cationic Nanoparticle-Assisted NMR Spin Relaxation.
Broadband Dynamics of Ubiquitin by Anionic and Cationic Nanoparticle-Assisted NMR Spin Relaxation.
Angew Chem Int Ed Engl. 2020 Sep 09;:
Authors: Wardenfelt S, Xiang X, Xie M, Yu L, Bruschweiler-Li L, Bruschweiler R
Abstract
The quantitative and comprehensive description of the internal dynamics of proteins is critical for understanding their function. Nanoparticle-assisted 15 N NMR spin relaxation is a new method that uses a...
[NMR paper] Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study
Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
Related Articles Side chain dynamics in unfolded protein states: an NMR based 2H spin relaxation study of delta131delta.
J Am Chem Soc. 2003 Feb 19;125(7):1748-58
Authors: Choy WY, Shortle D, Kay LE
NMR relaxation data on disordered proteins can provide insight into both structural and dynamic properties of these molecules. Because of chemical shift degeneracy in correlation spectra, detailed site-specific analyses of side chain dynamics...
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[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...
Observation of Sub-Microsecond Protein Methyl-Side Chain Dynamics by Nanoparticle-Assisted NMR Spin Relaxation
Linear Mode
