BACKGROUND: In-cell NMR is a valuable technique for investigating protein structure and function in cellular environments. However, challenges arise due to highly crowded cellular environment, where nonspecific interactions between the target protein and other cellular components can lead to signals broadening or disappearance in NMR spectra.
[NMR paper] Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-advances.gif Targeting the cryptic sites: NMR-based strategy to improve protein druggability by controlling the conformational equilibrium.
Sci Adv. 2020 Sep;6(40):
Authors: Mizukoshi Y, Takeuchi K, Tokunaga Y, Matsuo H, Imai M, Fujisaki M, Kamoshida H, Takizawa T, Hanzawa H, Shimada I
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[NMR paper] Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
Related Articles Effective strategy to assign (1)H- (15)N heteronuclear correlation NMR signals from lysine side-chain NH3 (+) groups of proteins at low temperature.
J Biomol NMR. 2014 Aug 17;
Authors: Esadze A, Zandarashvili L, Iwahara J
Abstract
Recent studies have shown that lysine side-chain NH3 (+) groups are excellent probes for NMR investigations of dynamics involving...
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08-19-2014 11:21 AM
Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature
Effective strategy to assign 1H-15N heteronuclear correlation NMR signals from lysine side-chain NH3 + groups of proteins at low temperature
Abstract
Recent studies have shown that lysine side-chain NH3 + groups are excellent probes for NMR investigations of dynamics involving hydrogen bonds and ion pairs relevant to protein function. However, due to rapid hydrogen exchange, observation of 1H-15N NMR cross peaks from lysine NH3 + groups often requires use of a relatively low temperature, which...
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08-16-2014 10:26 PM
[NMR paper] Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Investigation of Lysine Side Chain Interactions of Interleukin-8 with Heparin and other Glycosaminoglycans Studied by a Methylation-NMR Approach.
Glycobiology. 2013 Aug 27;
Authors: Möbius K, Nordsieck K, Pichert A, Samsonov SA, Thomas L, Schiller J, Kalkhof S, Pisabarro MT, Beck-Sickinger AG, Huster D
Abstract
Although the interaction between interleukin-8 (IL-8) and glycosaminoglycans (GAG) is...
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08-29-2013 01:53 PM
Lysine methylation strategies for characterizing protein conformations by NMR
Lysine methylation strategies for characterizing protein conformations by NMR
Abstract In the presence of formaldehyde and a mild reducing agent, reductive methylation is known to achieve near complete dimethylation of protein amino groups under non-denaturing conditions, in aqueous media. Amino methylation of proteins is employed in mass spectrometric, crystallographic, and NMR studies. Where biosynthetic labeling is prohibitive, amino 13C-methylation provides an attractive option for monitoring folding, kinetics, proteinâ??protein and protein-DNA interactions by NMR. Here, we...
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09-10-2012 01:48 AM
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Site-Specific Mapping and Time-Resolved Monitoring of Lysine Methylation by High-Resolution NMR Spectroscopy
Franc?ois-Xavier Theillet, Stamatios Liokatis, Jan Oliver Jost, Beata Bekei, Honor May Rose, Andres Binolfi, Dirk Schwarzer and Philipp Selenko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja301895f/aop/images/medium/ja-2012-01895f_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja301895f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/tV2dPnMa4Qc
Lysine methylation: A strategy to improve in-cell NMR spectroscopy of proteins
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