Nuclear Magnetic Resonance (NMR) is a tool of choice to characterize molecular motions. In biological macromolecules, pico- to nanosecond motions, in particular, can be probed by nuclear spin relaxation rates, which depend on the time fluctuations of the orientations of spin interaction frames. For the past 40 years, relaxation rates have been successfully analyzed using the Model-Free (MF) approach, which makes no assumption on the nature of motions and reports on the effective amplitude and...
[NMR paper] Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
Related Articles Motions and Entropies in Proteins as Seen in NMR Relaxation Experiments and Molecular Dynamics Simulations.
J Phys Chem B. 2014 Oct 28;
Authors: Allnér O, Foloppe N, Nilsson L
Abstract
Molecular dynamics simulations of E. coli glutaredoxin1 in water have been performed to relate the dynamical parameters and entropy obtained in NMR relaxation experiments, with results extracted from simulated trajectory...
nmrlearner
Journal club
0
10-29-2014 03:51 PM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
Related Articles Slow motions in microcrystalline proteins as observed by MAS-dependent (15)N rotating-frame NMR relaxation.
J Magn Reson. 2014 Sep 20;248C:8-12
Authors: Krushelnitsky A, Zinkevich T, Reif B, Saalwächter K
Abstract
(15)N NMR relaxation rate R1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s-ms...
nmrlearner
Journal club
0
10-06-2014 12:37 PM
[NMR paper] Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation
Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation
Publication date: Available online 20 September 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Alexey Krushelnitsky , Tatiana Zinkevich , Bernd Reif , Kay Saalwächter</br>
15N NMR relaxation rate R 1? measurements reveal that a substantial fraction of residues in the microcrystalline chicken alpha-spectrin SH3 domain protein undergoes dynamics in the ?s - ms timescale range. On the basis of a comparison of 2D site-resolved with 1D integrated 15N...
nmrlearner
Journal club
0
09-20-2014 07:51 PM
[NMR paper] NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
NMR Relaxation in Proteins with Fast Internal Motions and Slow Conformational Exchange: Model Free Framework and Markov State Simulations.
J Phys Chem B. 2013 May 2;
Authors: Xia J, Deng NJ, Levy RM
Abstract
Calculating NMR relaxation effects for proteins with dynamics on multiple timescales generally requires very long trajectories based on conventional molecular dynamics simulations. In this report,...
nmrlearner
Journal club
0
05-04-2013 09:18 PM
[Question from NMRWiki Q&A forum] How to process and analyze serial 1D data nmrPipe?
How to process and analyze serial 1D data nmrPipe?
Hi all,I am very new to nmrPipe. I want to achieve the following steps. It would be very kind if somebody helps.
I have a 2D bruker data (t2= 4k points, t1= 32 points) and I want to do Fourier transform in the F2 dimension,phase etc. (2) and then extract the 32 spectra as 1Ds and also convert these 32 spectra in ascii format.(3) fit the peaks with a gaussian or Lorentzian function.(4) integrate the peak and save the integrals and time points as an ascii file.
I only managed till the 1st step.Please help..!!
Explicit models of motions to analyze NMR relaxation data in proteins
Linear Mode
