1H, 13C, and 15N resonance assignments of Fusarium solani pisi cutinase and preliminary features of the structure in solution

Protein Science

Volumn 6, Issue 11, 1997, Pages 2375-2384

  Prompers, Jeanine J ^a   Groenewegen, Anneke ^b   Van Schaik, René C ^b   Pepermans, Henri A M ^b   Hilbers, Cornelis W ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b UNILEVER RESEARCH VLAARDINGEN   (Netherlands)

Author keywords

Amide aromatic hydrogen bond; Cutinase; Heteronuclear 3D NMR; Protein; Resonance assignment; Secondary structure

Indexed keywords

AMIDE; AROMATIC COMPOUND; CARBON 13; ENZYME; HYDROGEN; NITROGEN 15; AMINO ACID; CARBON; CARBOXYLESTERASE; CUTINASE; NITROGEN;

ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; ENZYME STRUCTURE; FUSARIUM SOLANI; HYDROGEN BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; FUSARIUM; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; SOLUTION AND SOLUBILITY;

ESCHERICHIA COLI; FUSARIUM; FUSARIUM SOLANI;

AMINO ACID SEQUENCE; AMINO ACIDS; CARBON ISOTOPES; CARBOXYLIC ESTER HYDROLASES; FUSARIUM; HYDROGEN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

EID: 0030609147     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061111     Document Type: Article

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