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A calorimetric study of the thermal stability of barstar and its interaction with barnase

Biochemistry

Apr 18, 1995

José Cifrián MartínezAlan R Fersht

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Abstract

The temperature-induced unfolding of single, double, and triple mutants of barstar, the specific intracellular protein inhibitor of barnase from Bacillus amyloliquefaciens, has been studied by high-sensitivity differential scanning calorimetry. The thermal unfolding of barstar mutants, ...read more

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Cysteine
Thermodynamics
Mutant
Bacillus amyloliquefaciens ribonuclease
Bacterial Proteins
Buffers
Alanine
Hydrogen-Ion Concentration
Calorimetry
Bacillus amyloliquefaciens
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A calorimetric study of the thermal stability of barstar and its interaction with barnase

Biochemistry

Apr 18, 1995

José Cifrián MartínezAlan R Fersht

PMID: 7711042

DOI: 10.1021/bi00015a036

Abstract

The temperature-induced unfolding of single, double, and triple mutants of barstar, the specific intracellular protein inhibitor of barnase from Bacillus amyloliquefaciens, has been studied by high-sensitivity differential scanning calorimetry. The thermal unfolding of barstar mutants, ...read more

Mentioned in this Paper

Cysteine
Thermodynamics
Mutant
Bacillus amyloliquefaciens ribonuclease
Bacterial Proteins

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