Proteins awakened from deep sleep to study their motions - Biotechin.Asia
Proteins awakened from deep sleep to study their motions - Biotechin.Asia
Proteins awakened from deep sleep to study their motions Biotechin.Asia
For the first time ever, scientists from PFL, IBS-Grenoble, and ENS-Lyon have captured the â??awakeningâ?? of a protein, that is to say, its gradual shift from an inert state to a functional state using an NMR spectroscopy device. The breakthrough approach ...
Waking proteins up from deep sleep to study their motions - Phys.Org
Waking proteins up from deep sleep to study their motions - Phys.Org
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Waking proteins up from deep sleep to study their motions
Phys.Org
In order to carry out their functions, proteins need to move. Scientists at EPFL have developed a new technique to study motions in proteins with unprecedented accuracy. The method, which is based on NMR, freezes proteins down to immobility, then ...
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04-30-2015 09:13 PM
[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...
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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...
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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...
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09-20-2014 07:51 PM
NanosecondTime Scale Motions in Proteins Revealedby High-Resolution NMR Relaxometry
NanosecondTime Scale Motions in Proteins Revealedby High-Resolution NMR Relaxometry
Cyril Charlier, Shahid Nawaz Khan, Thorsten Marquardsen, Philippe Pelupessy, Volker Reiss, Dimitris Sakellariou, Geoffrey Bodenhausen, Frank Engelke and Fabien Ferrage
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja409820g/aop/images/medium/ja-2013-09820g_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja409820g
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/QcFGZznyEp0
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11-27-2013 01:50 AM
[NMR paper] Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
Related Articles Nanosecond timescale motions in proteins revealed by high-resolution NMR relaxometry.
J Am Chem Soc. 2013 Nov 14;
Authors: Charlier CD, Khan SN, Marquardsen T, Pelupessy P, Reiss V, Sakellariou D, Bodenhausen G, Engelke F, Ferrage F
Abstract
Understanding the molecular determinants underlying protein function requires the characterization of both structure and dynamics at atomic resolution. Nuclear relaxation rates allow a precise...
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11-16-2013 03:14 PM
[NMR paper] High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritell
High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Related Articles High pressure nmr study of dihydrofolate reductase from a deep-sea bacterium Moritella profunda.
Cell Mol Biol (Noisy-le-grand). 2004 Jun;50(4):311-6
Authors: Hata K, Kono R, Fujisawa M, Kitahara R, Kamatari YO, Akasaka K, Xu Y
We have investigated the effect of pressure and temperature on the structural and thermodynamic stability of a protein dihydrofolate reductase from a deep-sea bacterium Moritella profunda in its folate-bound...
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11-24-2010 09:51 PM
Research Groups in Asia
Research Groups in AsiaDepartment of Chemical Physics, The Weizmann Institute of Science, Israel
Frydman Group, Weizmann Institute, Rehovot, Israel
Research in our group focuses on the development of new techniques
in nuclear magnetic resonance (NMR) analysis, and on the application of
these and other advanced methods to the resolution of chemical problems.
Most of this work is carried out in our three laboratory-built NMR spectrometers
(4.7, 7.2 and 11.8 T double- and triple-tuned instruments), which are equipped
with an array of solution, solid phase and microimaging accessories....