[NMR paper] A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
Related ArticlesA chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
J Biomol NMR. 2015 Feb 19;
Authors: Anderson KM, Nguyen D, Esadze A, Zandrashvili L, Gorenstein DG, Iwahara J
Abstract
Protein-nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three protein-DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allows for identification of NMR signals from the protein side-chain NH3 (+) groups forming the intermolecular ion pairs. A characteristic change in their (1)H and (15)N resonances upon this modification (i.e., substitution of phosphate to phosphorodithioate) can represent a signature of an intermolecular ion pair. Hydrogen-bond scalar coupling between protein side-chain (15)N and DNA phosphorodithiaote (31)P nuclei provides direct confirmation of the intermolecular ion pair. The same approach is likely applicable to protein-RNA complexes as well.
PMID: 25690740 [PubMed - as supplied by publisher]
A chemical approach for site-specific identification of NMR signals from protein side-chain NH 3 + groups forming intermolecular ion pairs in proteinâ??nucleic acid complexes
A chemical approach for site-specific identification of NMR signals from protein side-chain NH 3 + groups forming intermolecular ion pairs in proteinâ??nucleic acid complexes
Abstract
Proteinâ??nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three proteinâ??DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allows for identification of NMR signals from the protein side-chain NH3 + groups forming the...
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02-18-2015 06:15 PM
[NMR paper] Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Related Articles Accurate ab initio prediction of NMR chemical shifts of nucleic acids and nucleic acids/protein complexes.
Nucleic Acids Res. 2014 Nov 17;
Authors: Victora A, Möller HM, Exner TE
Abstract
NMR chemical shift predictions based on empirical methods are nowadays indispensable tools during resonance assignment and 3D structure calculation of proteins. However, owing to the very limited statistical data basis,...
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11-19-2014 04:32 PM
[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
Specific Labeling of ThreonineMethyl Groups for NMR Studies of Protein–Nucleic Acid Complexes
Specific Labeling of ThreonineMethyl Groups for NMR Studies of Protein–Nucleic Acid Complexes
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201496d/aop/images/medium/bi-2011-01496d_0001.gif
Biochemistry
DOI: 10.1021/bi201496d
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11-04-2011 03:17 AM
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Binding site identification and structure determination of protein-ligand complexes by NMR a semiautomated approach.
Methods Enzymol. 2011;493:241-75
Authors: Ziarek JJ, Peterson FC, Lytle BL, Volkman BF
Over the last 15years, the role of NMR spectroscopy in the lead identification and optimization stages of pharmaceutical drug discovery has steadily increased. NMR occupies a unique niche in the biophysical analysis of drug-like...
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03-05-2011 01:02 PM
Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membra
Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
Related Articles Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
Protein Sci. 2010 Nov 15;
Authors: Shi P, Wang H, Xi Z, Shi C, Xiong Y, Tian C
Site-specific (19)F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one dimensional (19)F spectra and T(1), T(2) relaxation data were acquired...
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11-17-2010 05:49 PM
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analy
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Related Articles Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Biochem Biophys Res Commun. 2010 Oct 11;
Authors: Shi P, Xi Z, Wang H, Shi C, Xiong Y, Tian C
SH3 is a ubiquitous domain mediating protein-protein interactions....
A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes.
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