New limits of sensitivity of site-directed spin labeling electron paramagnetic resonance for membrane proteins #DNPNMR
From The DNP-NMR Blog:
New limits of sensitivity of site-directed spin labeling electron paramagnetic resonance for membrane proteins #DNPNMR
A nice overview how spinlabels can be used for structural biology studies. This includes pulsed EPR techniques such as PELDOR (DEER) and ODNP spectroscopy.
Bordignon, Enrica, and Stephanie Bleicken. “New Limits of Sensitivity of Site-Directed Spin Labeling Electron Paramagnetic Resonance for Membrane Proteins.” Biochimica et Biophysica Acta (BBA) - Biomembranes 1860, no. 4 (April 2018): 841–53. https://doi.org/10.1016/j.bbamem.2017.12.009.
[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
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
Chemoselective and Site-Selective Lysine-Directed Lysine Modification Enables Single-Site Labeling of Native Proteins
Linear Mode
