The role of quaternary interactions on the stability and activity of ascorbate peroxidase

Protein Science

Volumn 7, Issue 10, 1998, Pages 2089-2098

  Mandelman, David ^a   Schwarz, Frederick P ^b   Li, Huiying ^a   Poulos, Thomas L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY   (United States)

Author keywords

Ascorbate peroxidase; Differential scanning calorimetry; Quaternary structure; Salt bridges; Solvent structure; Subunit interface; Thermostability

Indexed keywords

ASCORBATE PEROXIDASE; ASCORBIC ACID; DIMER; UNCLASSIFIED DRUG;

ABSORPTION SPECTROPHOTOMETRY; ARTICLE; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; DIMERIZATION; ENTHALPY; ENZYME ACTIVITY; ENZYME STABILITY; POINT MUTATION; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; THERMOSTABILITY;

EID: 0031789162     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071005     Document Type: Article

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