Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase/protease I: A member of a new subclass of lipolytic enzymes

Journal of Biomolecular NMR

Volumn 11, Issue 4, 1998, Pages 363-380

  Lin, Ta Hsien ^a,c   Chen, Chinpan ^a   Huang, Rong Fong ^a   Lee, Ya Lin ^b   Shaw, Jei Fu ^b   Huang, Tai Huang ^a  

^a Institute of Biomedical Science   (Taiwan)

^b INSTITUTE OF PLANT AND MICROBIAL BIOLOGY   (Taiwan)

^c TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

Author keywords

Chemical shift indices; Heteronuclear triple resonance NMR; Lipase; Lipolytic enzyme; Resonance assignment

Indexed keywords

ESCHERICHIA COLI;

CARBON; ESCHERICHIA COLI PERIPLASMIC PROTEINASE; MULTIENZYME COMPLEX; NITROGEN; SERINE PROTEINASE; THIOL ESTER HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ESCHERICHIA COLI; ISOTOPE LABELING; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; CARBON ISOTOPES; ESCHERICHIA COLI; ISOTOPE LABELING; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SERINE ENDOPEPTIDASES; THIOLESTER HYDROLASES;

EID: 0032058947     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008226515482     Document Type: Article

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