[NMR paper] Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis
Molecular Dynamics-Assisted Optimization of Protein NMR Relaxation Analysis
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...
More...
nmrlearner
Journal club
0
03-05-2022 01:44 AM
[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
nmrlearner
Journal club
0
08-26-2021 06:47 AM
[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] 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] Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Multiple Scale Dynamics in Proteins Probed at Multiple Time Scales through Fluctuations of NMR Chemical Shifts.
J Phys Chem B. 2014 Mar 14;
Authors: Calligari PA, Abergel D
Abstract
Fluctuations of NMR resonance frequency shifts and their relation with protein exchanging conformations are usually...
Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation - Science
Linear Mode
