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DSC studies of the conformational stability of barstar wild-type

Protein Science : a Publication of the Protein Society

Oct 1, 1997

A SchöppeJayant B Udgaonkar

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Abstract

The temperature induced unfolding of barstar wild-type of bacillus amyloliquefaciens (90 residues) has been characterized by differential scanning microcalorimetry. The process has been found to be reversible in the pH range from 6.4 to 8.3 in the absence of oxygen. It has been clearly ...read more

Mentioned in this Paper

Sulfhydryl Reagents
Thermodynamics
Mutant
Bacillus amyloliquefaciens ribonuclease
Drug Stability
Denaturation
Microcalorimetry
Bacterial Proteins
Protein Conformation
Hydrogen-Ion Concentration
Paper Details
References
  • References17
  • Citations6
12

DSC studies of the conformational stability of barstar wild-type

Protein Science : a Publication of the Protein Society

Oct 1, 1997

A SchöppeJayant B Udgaonkar

PMID: 9336842

DOI: 10.1002/pro.5560061014

Abstract

The temperature induced unfolding of barstar wild-type of bacillus amyloliquefaciens (90 residues) has been characterized by differential scanning microcalorimetry. The process has been found to be reversible in the pH range from 6.4 to 8.3 in the absence of oxygen. It has been clearly ...read more

Mentioned in this Paper

Sulfhydryl Reagents
Thermodynamics
Mutant
Bacillus amyloliquefaciens ribonuclease
Drug Stability

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Paper Details
References
  • References17
  • Citations6
12

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