NMR Assignment of 2H, 13C and 15N labeled amino-terminal domain of apo-pantothenate synthetase from E. coli [36]

Journal of Biomolecular NMR

Volumn 36, Issue SUPPL. 1, 2006, Pages 38-

  Chakrabarti, Kalyan Sundar ^a   Sarma, Siddhartha P ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 13; ESCHERICHIA COLI PROTEIN; NITROGEN 15; PANTOTHENATE SYNTHETASE; UNCLASSIFIED DRUG; APOENZYME; PEPTIDE SYNTHASE; RECOMBINANT PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; BETA SHEET; CARBON NUCLEAR MAGNETIC RESONANCE; CATALYSIS; DEUTERON NUCLEAR MAGNETIC RESONANCE; ESCHERICHIA COLI; LETTER; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; CHEMISTRY; ENZYME ACTIVE SITE; MOLECULAR CLONING; NUCLEAR MAGNETIC RESONANCE; PROTEIN SECONDARY STRUCTURE;

APOENZYMES; CATALYTIC DOMAIN; CLONING, MOLECULAR; ESCHERICHIA COLI PROTEINS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE SYNTHASES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 34250323810     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-006-9005-1     Document Type: Letter

References (2)

1. Brown et al. (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology, Neidhart, F. C. (Ed.), A.S.M., Washington (D.C), pp. 521-538
2. Yamazaki et al. (1994) JACS, 116, 1656-11666.