Dimethyl sulfoxide at 2.5% (v/v) alters the structural cooperativity and unfolding mechanism of dimeric bacterial NAD+ synthetase

Protein Science

Volumn 13, Issue 3, 2004, Pages 830-841

  Yang, Zhengrong W ^a   Tendian, Susan W ^a   Carson, W Michael ^a,b   Brouillette, Wayne J ^a   Delucas, Lawrence J ^a   Brouillette, Christie G ^a,c  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

^b and Radiation Oncology   (United States)

^c CBSE 234   (United States)

Author keywords

Analytical ultracentrifugation; Compound screening; Differential scanning calorimetry; Dimerization; DMSO; Protein folding; Structural cooperativity

Indexed keywords

BACTERIAL ENZYME; DIMER; DIMETHYL SULFOXIDE; MONOMER; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG;

ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; HYDRODYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; ULTRACENTRIFUGATION;

ALGORITHMS; AMIDE SYNTHASES; BACILLUS SUBTILIS; BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; DIMETHYL SULFOXIDE; ENZYME STABILITY; MODELS, CHEMICAL; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; RECOMBINANT PROTEINS; THERMODYNAMICS; ULTRACENTRIFUGATION;

BACTERIA (MICROORGANISMS);

EID: 1342310505     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03330104     Document Type: Article

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