[ASAP] Assessing Site-Specific Enhancements Imparted by Hyperpolarized Water in Folded and Unfolded Proteins by 2D HMQC NMR
Assessing Site-Specific Enhancements Imparted by Hyperpolarized Water in Folded and Unfolded Proteins by 2D HMQC NMR
Or Szekely†?, Gregory Lars Olsen†§, Mihajlo Novakovic†, Rina Rosenzweig‡, and Lucio Frydman*†
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c00807/20200512/images/medium/ja0c00807_0012.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c00807
http://feeds.feedburner.com/~r/acs/jacsat/~4/Wg_2GlL7qPY
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[NMR paper] Assessing site-specific enhancements imparted by hyperpolarized water in folded and unfolded proteins by 2D HMQC NMR.
Assessing site-specific enhancements imparted by hyperpolarized water in folded and unfolded proteins by 2D HMQC NMR.
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J Am Chem Soc. 2020 Apr 27;:
Authors: Szekely O, Olsen GL, Novakovic M, Rosenzweig R, Frydman L
Abstract
Dissolution DNP of hyperpolarized water can be a valuable aid in biomolecular NMR. With suitable optimizations one can utilize it to achieve, under near-physiological...
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Structural biology: Proteins in dynamic equilibrium - Nature.com
Structural biology: Proteins in dynamic equilibrium - Nature.com
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Structural biology: Proteins in dynamic equilibrium
Nature.com
Changes in global orientations of protein domains, or in the shape and size of molecular assemblies, are more difficult to characterize using NMR alone, ...
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