Protein-protein interaction revealed by NMR T2 relaxation experiments: The lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus

Journal of Molecular Biology

Volumn 295, Issue 4, 2000, Pages 1023-1037

  Howard, Mark J ^a   Chauhan, Hitesh J ^a   Domingo, Gonzalo J ^a   Fuller, Christopher ^a   Perham, Richard N ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Lipoic acid; Multienzyme complex; Protein protein interaction; Pyruvate dehydrogenase; T2 relaxation

Indexed keywords

ACYLTRANSFERASE; DIHYDROLIPOAMIDE DEHYDROGENASE; PYRUVATE DEHYDROGENASE; THIOCTIC ACID;

ACETYLATION; ARTICLE; BACTERIAL GROWTH; CATALYSIS; ESCHERICHIA COLI; GENE OVEREXPRESSION; GEOBACILLUS STEAROTHERMOPHILUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SITE DIRECTED MUTAGENESIS;

EID: 0034723135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3391     Document Type: Article

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