Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy
Improved accuracy in measuring one-bond and two-bond 15N,13Cα coupling constants in proteins by double-inphase/antiphase (DIPAP) spectroscopy
Abstract An extension to HN(CO-α/β-N,Cα-J)-TROSY (Permi and Annila in J Biomol NMR 16:221â??227, 2000) is proposed that permits the simultaneous determination of the four coupling constants 1 J Nâ?²(i)Cα(i), 2 J HN(i)Cα(i), 2 J Cα(iâ??1)Nâ?²(i), and 3 J Cα(iâ??1)HN(i) in 15N,13C-labeled proteins. Contrasting the original scheme, in which two separate subspectra exhibit the 2 J CαNâ?² coupling as inphase and antiphase splitting (IPAP), we...
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Solid-State 91Zr NMR Spectroscopy Studies of Zirconocene Olefin Polymerization Catalyst Precursors
Solid-State 91Zr NMR Spectroscopy Studies of Zirconocene Olefin Polymerization Catalyst Precursors
Aaron J. Rossini, Ivan Hung, Samuel A. Johnson, Carla Slebodnick, Mike Mensch, Paul A. Deck and Robert W. Schurko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107749b/aop/images/medium/ja-2010-07749b_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107749b
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/GGw8Igo70Jo
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[NMR paper] NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed wi
NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.
Related Articles NMR structure of a bifunctional rhodamine labeled N-domain of troponin C complexed with the regulatory "switch" peptide from troponin I: implications for in situ fluorescence studies in muscle fibers.
Biochemistry. 2003 Apr 22;42(15):4333-48
Authors: Mercier P, Ferguson RE, Irving M, Corrie JE, Trentham DR, Sykes BD
The structure...
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11-24-2010 09:01 PM
[NMR paper] 13C NMR chemical shifts can predict disulfide bond formation.
13C NMR chemical shifts can predict disulfide bond formation.
Related Articles 13C NMR chemical shifts can predict disulfide bond formation.
J Biomol NMR. 2000 Oct;18(2):165-71
Authors: Sharma D, Rajarathnam K
The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the reduced (free) and oxidized (disulfide bonded)...
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11-19-2010 08:29 PM
[NMR paper] Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the
Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
Related Articles Novel mechanism of surface catalysis of protein adduct formation. NMR studies of the acetylation of ubiquitin.
J Biol Chem. 2000 Oct 13;275(41):31908-13
Authors: Macdonald JM, Haas AL, London RE
Reactivity of surface lysyl residues of proteins with a broad range of chemical agents has been proposed to be dependent on the catalytic microenvironment of the residue. We have investigated the acetylation of wild type...
NMR Spectroscopist - Chemical and Catalyst Science - Golden, Colorado
The NREL are looking for a NMR Spectroscopist (taken from the American Chemical Society's website - chemistryjobs.acs.org )
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The National Renewable Energy Laboratory (NREL), located in beautiful Golden, Colorado, is a leader in the U.S. Department of Energy’s effort to secure an energy future for the nation that is environmentally and economically sustainable. Our mission is to develop renewable energy and energy efficiency technologies and practices, advance related science and engineering and transfer knowledge and innovations to address the nation’s energy and...
Mechanism of Enantioselective C-C Bond Formation with Bifunctional Chiral Ru Catalyst
Linear Mode
