NMR relaxation analysis of the mobile residues in globular proteins is sensitive to the form of the experimentally fitted internal autocorrelation function, which is used to represent that motion. Different order parameter representations can precisely fit the same set of ^(15)N R(1), R(2), and heteronuclear NOE measurements while yielding significantly divergent predictions of the underlying autocorrelation functions, indicating the insufficiency of these experimental relaxation data for...
[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] 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
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...
[NMR paper] Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation.
Adv Exp Med Biol. 2015;842:217-30
Authors: Zhang Y, Yamaguchi T, Satoh T, Yagi-Utsumi M, Kamiya Y,...
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[NMR paper] General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
Related Articles General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations.
Biochem Biophys Res Commun. 2015 Jan 16;
Authors: Liu Q, Shi C, Yu L, Zhang L, Xiong Y, Tian C
Abstract
Internal backbone dynamic motions are essential for different protein functions and...
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General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations
General Order Parameter based Correlation Analysis of Protein Backbone Motions between Experimental NMR Relaxation Measurements and Molecular Dynamics Simulations
Publication date: Available online 16 January 2015
Source:Biochemical and Biophysical Research Communications</br>
Author(s): Qing Liu , Chaowei Shi , Lu Yu , Longhua Zhang , Ying Xiong , Changlin Tian</br>
Internal backbone dynamic motions are essential for different protein functions and occur on a wide range of time scales, from femtoseconds to seconds. Molecular dynamic (MD) simulations and...
Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis
Linear Mode
