[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
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05-01-2018 10:57 PM
[NMR paper] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Related Articles Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes as Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations.
Biochemistry. 2018 Apr 17;:
Authors: Baird-Titus JM, Thapa M, Doerdelmann T, Combs KA, Rance M
Abstract
An important but poorly characterized contribution to the thermodynamics of protein-DNA interactions is...
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04-18-2018 01:41 PM
Site-selective 13 C labeling of proteins using erythrose
Site-selective 13 C labeling of proteins using erythrose
Abstract
NMR-spectroscopy enables unique experimental studies on protein dynamics at atomic resolution. In order to obtain a full atom view on protein dynamics, and to study specific local processes like ring-flips, proton-transfer, or tautomerization, one has to perform studies on amino-acid side chains. A key requirement for these studies is site-selective labeling with 13C and/or 1H, which is achieved in the most general way by using site-selectively 13C-enriched glucose (1- and 2-13C) as the...
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03-01-2017 04:13 AM
[NMR paper] A Versatile Approach for Site-Specific Lysine Acylation in Proteins
A Versatile Approach for Site-Specific Lysine Acylation in Proteins
Using amber suppression in coordination with a mutant pyrrolysyl-tRNA synthetase-tRNAPyl pair, azidonorleucine is genetically encoded in E. coli. Its genetic incorporation followed by traceless Staudinger ligation with a phosphinothioester allows the convenient synthesis of a protein with a site-specifically installed lysine acylation. By simply changing the phosphinothioester identity, any lysine acylation type could be introduced. Using this approach, we demonstrated that both lysine acetylation and lysine...
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01-02-2017 10:17 AM
Gd(iii) and Mn(ii) complexes for dynamic nuclear polarization: small molecular chelate polarizing agents and applications with site-directed spin labeling of proteins #DNPNMR
From The DNP-NMR Blog:
Gd(iii) and Mn(ii) complexes for dynamic nuclear polarization: small molecular chelate polarizing agents and applications with site-directed spin labeling of proteins #DNPNMR
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Kaushik, M., et al., Gd(iii) and Mn(ii) complexes for dynamic nuclear polarization: small molecular chelate polarizing agents and applications with site-directed spin labeling of proteins. Phys Chem Chem Phys, 2016. 18(39): p. 27205-27218.
https://www.ncbi.nlm.nih.gov/pubmed/27545112
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11-19-2016 08:35 PM
[NMR paper] Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Related Articles Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling.
Chemistry. 2015 Sep 7;21(37):12971-7
Authors: van der Cruijsen EA, Koers EJ, Sauvée C, Hulse RE, Weingarth M, Ouari O, Perozo E, Tordo P, Baldus M
Abstract
Dynamic nuclear polarization (DNP) has been shown to greatly enhance spectroscopic sensitivity, creating novel opportunities for NMR studies on complex and large molecular assemblies in life and material...
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09-01-2015 10:48 AM
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling
From The DNP-NMR Blog:
Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling
van der Cruijsen, E.A.W., et al., Biomolecular DNP-Supported NMR Spectroscopy using Site-Directed Spin Labeling. Chemistry – A European Journal, 2015: p. n/a-n/a.
http://dx.doi.org/10.1002/chem.201501376
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08-11-2015 02:50 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
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Chemoselective and Site-Selective Lysine-Directed Lysine Modification Enables Single-Site Labeling of Native Proteins
Linear Mode
