Related Articles(1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
Biomol NMR Assign. 2013 Apr;7(1):1-4
Authors: Nogaret S, Guittet E, Birlirakis N
Abstract
CGC-19, a 14 kDa proteic constituent of a non ribosomal peptide synthetase implicated in the biosynthesis of a secondary metabolite in Streptomyces ambofaciens, has been isotopically enriched and recombinantly expressed. Its nearly complete (1)H, (13)C and (15)N resonance assignment is reported hereunder.
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NMR Structure of the C-Terminal Domain of a Tyrosyl-tRNA Synthetase That Functions in Group I Intron Splicing
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200189u/aop/images/medium/bi-2011-00189u_0010.gif
Biochemistry
DOI: 10.1021/bi200189u
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NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing.
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Biochemistry. 2011 Mar 25;
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(1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
Linear Mode
