1H, 13C and 15N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase
Autor: | Nicolas Birlirakis, Eric Guittet, Sophie Nogaret |
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Přispěvatelé: | Institut de Chimie des Substances Naturelles (ICSN), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC) |
Rok vydání: | 2012 |
Předmět: |
Streptomyces ambofaciens
Stereochemistry Molecular Sequence Data Peptide Biology Secondary metabolite 01 natural sciences Biochemistry Protein Structure Secondary 03 medical and health sciences chemistry.chemical_compound Biosynthesis Structural Biology medicine Amino Acid Sequence Peptide Synthases Nuclear Magnetic Resonance Biomolecular 030304 developmental biology chemistry.chemical_classification 0303 health sciences [CHIM.ORGA]Chemical Sciences/Organic chemistry 010405 organic chemistry Resonance Ribosomal RNA Peptide Fragments Protein Structure Tertiary 0104 chemical sciences chemistry medicine.drug |
Zdroj: | Biomolecular NMR Assignments Biomolecular NMR Assignments, Springer, 2013, 7 (1), pp.1-4. ⟨10.1007/s12104-012-9364-3⟩ |
ISSN: | 1874-270X 1874-2718 |
Popis: | International audience; 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. |
Databáze: | OpenAIRE |
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