[NMR paper] Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
Related Articles Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
J Biomol Struct Dyn. 2014 Aug 8;:1-10
Authors: Zhang J, Wang F, Zhang Y
Abstract
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases that affect a wide variety of mammalian species such as sheep and...
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08-12-2014 06:25 PM
In SituNMR Spectroscopy of Supercapacitors: Insightinto the Charge Storage Mechanism
In SituNMR Spectroscopy of Supercapacitors: Insightinto the Charge Storage Mechanism
Hao Wang, Alexander C. Forse, John M. Griffin, Nicole M. Trease, Lorie Trognko, Pierre-Louis Taberna, Patrice Simon and Clare P. Grey
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja410287s/aop/images/medium/ja-2013-10287s_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja410287s
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ZN4MowZBRDs
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12-05-2013 06:19 AM
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
J Am Chem Soc. 2011 Mar 4;
Authors: Tang M, Sperling LJ, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM
Ubiquinone (Coenzyme Q) plays an important role in the mitochondrial respiratory chain and also acts as an antioxidant in its reduced form, protecting cellular membranes from peroxidation....
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03-08-2011 01:40 PM
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Ming Tang, Lindsay J. Sperling, Deborah A. Berthold, Anna E. Nesbitt, Robert B. Gennis and Chad M. Rienstra
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107775w/aop/images/medium/ja-2010-07775w_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107775w
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http://feeds.feedburner.com/~r/acs/jacsat/~4/WdFsSgH1V7w
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03-05-2011 02:44 AM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
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01-12-2011 11:11 AM
Post-Doc fellowship in NMR Methods to Study Ionic Solids/liquids - Univ. of Aveiro/Lisbon (Portugal)
Post-Doc fellowship in NMR Methods to Study Ionic Solids/liquids - Univ. of Aveiro/Lisbon (Portugal)
A 1-year postdoctoral position is available starting from January 2011, (extendable for additional 12 months) to study the “solid structure” of ionic liquids (ILs) and ionic solids (ISs) with relevance to the pharmaceutical industry. The research will be centred in the use of NMR techniques in tandem with molecular modelling to study the physical chemistry of molecular interactions in ILs and ISs. The project will be performed at the NMR centres at the Universities of Aveiro (solid state...
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12-01-2010 08:36 PM
[NMR paper] Rearrangement of charge-charge interactions in variant ubiquitins as detected by doub
Rearrangement of charge-charge interactions in variant ubiquitins as detected by double-mutant cycles and NMR.
Related Articles Rearrangement of charge-charge interactions in variant ubiquitins as detected by double-mutant cycles and NMR.
J Mol Biol. 2003 Sep 26;332(4):927-36
Authors: Sundd M, Robertson AD
Previous studies of ubiquitin disclosed numerous charge-charge interactions on the protein's surface. To investigate how neighboring residues influence the strength of these interactions, double-mutant cycles are combined with pK(a)...