Crystal structure and fluorescence studies reveal the role of helical dimeric interface of staphylococcal fabg1 in positive cooperativity for NADPH

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 4, 2012, Pages 1250-1257

  Dutta, Debajyoti ^a   Bhattacharyya, Sudipta ^a   Das, Amit Kumar ^a  

^a INDIAN INSTITUTE OF TECHNOLOGY   (India)

Author keywords

Dimerization axis; Fluorescence resonance energy transfer; Hypsochromic shift; Positive cooperativity; Staphylococcus aureus; Tryptophan fluorescence

Indexed keywords

BACTERIAL PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STAPHYLOCOCCUS AUREUS FABG1 PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CRYSTAL STRUCTURE; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION;

ALCOHOL OXIDOREDUCTASES; BACTERIAL PROTEINS; CLONING, MOLECULAR; CRYSTALLIZATION; DNA, BACTERIAL; ESCHERICHIA COLI; FLUORESCENCE; NADP; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; STAPHYLOCOCCUS AUREUS; TRYPTOPHAN;

STAPHYLOCOCCUS AUREUS;

EID: 84857792572     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24024     Document Type: Article

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