'Designing out' disulfide bonds: Thermodynamic properties of 30-51 cystine substitution mutants of bovine pancreatic trypsin inhibitor

Biochemistry

Volumn 36, Issue 18, 1997, Pages 5323-5335

  Liu, Yi ^a,b   Breslauer, Kenneth ^b,c   Anderson, Stephen ^a,b  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c RUTGERS CANCER INSTITUTE OF NEW JERSEY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; DISULFIDE BOND; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

AMINO ACID SEQUENCE; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; CATTLE; CIRCULAR DICHROISM; CYSTINE; DISULFIDES; DRUG DESIGN; ESCHERICHIA COLI; GUANIDINE; GUANIDINES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; TRYPSIN INHIBITOR, KAZAL PANCREATIC;

BOVINAE;

EID: 0030996965     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi962423c     Document Type: Article

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