Amino-acid substitutions at the fully exposed P1 site of bovine pancreatic trypsin inhibitor affect its stability

Protein Science

Volumn 10, Issue 4, 2001, Pages 715-724

  Krowarsch, Daniel ^a   Otlewski, Jacek ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Bovine pancreatic trypsin inhibitor; Reverse hydrophobic effect; Solvent exposed residue; Thermodynamic stability

Indexed keywords

AMINO ACID; APROTININ; CYSTEINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE BOND; ENERGY TRANSFER; ENZYME DENATURATION; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; THERMODYNAMICS;

AMINO ACID SUBSTITUTION; ANIMALS; APROTININ; CALORIMETRY, DIFFERENTIAL SCANNING; CATTLE; CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; PANCRELIPASE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; THERMODYNAMICS;

BOVINAE;

EID: 0035078662     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.38101     Document Type: Article

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