Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Ultra High-Resolution NMR: Sustained Induction Decays of Long-Lived Coherences
Aure?lien Bornet, Sami Jannin, J. A. (Ton) Konter, Patrick Hautle, Ben van den Brandt and Geoffrey Bodenhausen
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2052792/aop/images/medium/ja-2011-052792_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2052792
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/F3VMiSJp4h4
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09-02-2011 07:31 PM
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Chemphyschem. 2011 Aug 31;
Authors: Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR
Abstract
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain...
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09-02-2011 05:40 PM
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Narrowing the conformational space sampled by two-domain proteins with paramagnetic probes in both domains
Abstract Calmodulin is a two-domain protein which in solution can adopt a variety of conformations upon reorientation of its domains. The maximum occurrence (MO) of a set of calmodulin conformations that are representative of the overall conformational space possibly sampled by the protein, has been calculated from the paramagnetism-based restraints. These restraints were measured after inclusion of a lanthanide binding tag in the C-terminal domain to supplement the data obtained...
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08-13-2011 02:47 AM
Overexpression of a homogeneous oligosaccharide with 13C labeling by genetically engineered yeast strain
Overexpression of a homogeneous oligosaccharide with 13C labeling by genetically engineered yeast strain
Abstract This report describes a novel method for overexpression of 13C-labeled oligosaccharides using genetically engineered Saccharomyces cerevisiae cells, in which a homogeneous high-mannose-type oligosaccharide accumulates because of deletions of genes encoding three enzymes involved in the processing pathway of asparagine-linked oligosaccharides in the Golgi complex. Using uniformly 13C-labeled glucose as the sole carbon source in the culture medium of these engineered yeast...
[NMR paper] A high-resolution NMR study of long-lived water molecules in both oxidation states of
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Related Articles A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome c.
Biochemistry. 2003 Apr 1;42(12):3457-63
Authors: Bertini I, Ghosh K, Rosato A, Vasos PR
The interaction of water with oxidized and reduced cytochrome c from the Gram-positive bacterium Bacillus pasteurii (a 71-amino acid long monoheme cytochrome) is investigated through CLEANEX experiments and (15)N-edited...
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11-24-2010 09:01 PM
Long-Lived Coherences for Line-Narrowing in High-Field NMR
Long-Lived Coherences for Line-Narrowing in High-Field NMR
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 21 October 2010</br>
Riddhiman, Sarkar , Puneet, Ahuja , Paul R., Vasos , Aurélien, Bornet , Olivier, Wagnières , ...</br>
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10-22-2010 07:34 AM
[NMR thesis] NMR imaging of solids with multiple-pulse line narrowing and radiofrequency gradients
NMR imaging of solids with multiple-pulse line narrowing and radiofrequency gradients
Werner, Margat Hoppe (1993) NMR imaging of solids with multiple-pulse line narrowing and radiofrequency gradients. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-11212006-091334
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