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Journal of the American Chemical Society

Volumn 124, Issue 34, 2002, Pages 10025-10035

Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G

(4) Tugarinov, Vitali a Muhandiram, Ranjith a Ayed, Ayeda b Kay, Lewis E a

a UNIVERSITY OF TORONTO (Canada)

b UNIVERSITY OF TORONTO (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL SHIFT;

ENZYMES; ESCHERICHIA COLI; MONOMERS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS;

CHEMICAL ANALYSIS;

AMIDE; MALATE SYNTHASE;

ALPHA HELIX; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; CHEMICAL MODIFICATION; ESCHERICHIA COLI; LIGAND BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METHODOLOGY; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SOLUTION AND SOLUBILITY;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; MALATE SYNTHASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS; SUPPORT, NON-U.S. GOV'T;

EID: 0037189901 PISSN: 00027863 EISSN: None Source Type: Journal
DOI: 10.1021/ja0205636 Document Type: Article

Times cited : (211)

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