Publication date: April 2015 Source:Journal of Magnetic Resonance, Volume 253
Author(s): Enrico Ravera , Tobias Schubeis , Tommaso Martelli , Marco Fragai , Giacomo Parigi , Claudio Luchinat
Resolution and sensitivity in solid state NMR (SSNMR) can rival the results achieved by solution NMR, and even outperform them in the case of large systems. However, several factors affect the spectral quality in SSNMR samples, and not all systems turn out to be equally amenable for this methodology. In this review we attempt at analyzing the causes of this variable behavior and at providing hints to increase the chances of experimental success. Graphical abstract
[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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[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
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins
Abstract
Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diffusion, and can be affected by paramagnetic impurities as e.g. oxygen, which make a quantitative interpretation difficult. We present here the site-specific measurement of 13C and 15N heteronuclear rates in an immobilized protein. For methyls, a strong effect is expected due to the three-fold rotation of the methyl group. Quantification of the 13C...
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07-03-2014 06:04 AM
[NMR paper] Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits.
Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits.
Related Articles Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits.
Biochem Biophys Res Commun. 2014 Feb 10;
Authors: Lindert S, Maslennikov I, Chiu E, Pierce LC, Andrew McCammon J, Choe S
Abstract
About 8,000 genes encode membrane proteins in the human genome. The information about their druggability will be very useful to facilitate...
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Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits
Drug screening strategy for human membrane proteins: from NMR protein backbone structure to in silica- and NMR-screened hits
Publication date: Available online 10 February 2014
Source:Biochemical and Biophysical Research Communications</br>
Author(s): Steffen Lindert , Innokentiy Maslennikov , Ellis Chiu , Levi C Pierce , J. Andrew McCammon , Senyon Choe</br>
About 8,000 genes encode membrane proteins in the human genome. The information about their druggability will be very useful to facilitate drug discovery and development. The main problem, however,...
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02-10-2014 08:46 PM
Solid-state NMR of proteins sedimented by ultracentrifugation [Chemistry]
Solid-state NMR of proteins sedimented by ultracentrifugation
Bertini, I., Luchinat, C., Parigi, G., Ravera, E., Reif, B., Turano, P....
Date: 2011-06-28
Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when spinning is stopped, allowing one to study them in both conditions. Transiently sedimented proteins can be considered a...
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06-29-2011 04:45 AM
Solid-state NMR of proteins sedimented by ultracentrifugation.
Solid-state NMR of proteins sedimented by ultracentrifugation.
Solid-state NMR of proteins sedimented by ultracentrifugation.
Proc Natl Acad Sci U S A. 2011 Jun 13;
Authors: Bertini I, Luchinat C, Parigi G, Ravera E, Reif B, Turano P
Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when...
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06-15-2011 01:15 PM
[NMR paper] NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its
NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Related Articles NMR characterization of the metallo-beta-lactamase from Bacteroides fragilis and its interaction with a tight-binding inhibitor: role of an active-site loop.
Biochemistry. 1999 Nov 2;38(44):14507-14
Authors: Scrofani SD, Chung J, Huntley JJ, Benkovic SJ, Wright PE, Dyson HJ
Understanding the structure and dynamics of the enzymes that mediate antibiotic resistance of...
NMR of sedimented, fibrillized, silica-entrapped and microcrystalline (metallo)proteins
Linear Mode
