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Folding of subtilisin BPN': characterization of a folding intermediate

Biochemistry

Jan 12, 1993

J EderA R Fersht

PMID: 8418836

Abstract

Subtilisin BPN', an extracellular serine protease from Bacillus amyloliquefaciens, requires a 77 amino acid pro-sequence for correct folding in vivo. We report the observation of a metastable folding intermediate during the refolding of wild-type and a proteolytically inactive mutant su...read more

Mentioned in this Paper

In Vivo NMR Spectroscopy
Amides
Alkalescens-Dispar Group
Extracellular
Calcium
Mutagenesis, Site-Directed
Myxobacter alpha-lytic proteinase
Subtilisins
Bacillus amyloliquefaciens
Fluorescence Spectroscopy
35
Paper Details
References
  • References23
  • Citations55
12345...

Folding of subtilisin BPN': characterization of a folding intermediate

Biochemistry

Jan 12, 1993

J EderA R Fersht

PMID: 8418836

DOI:

Abstract

Subtilisin BPN', an extracellular serine protease from Bacillus amyloliquefaciens, requires a 77 amino acid pro-sequence for correct folding in vivo. We report the observation of a metastable folding intermediate during the refolding of wild-type and a proteolytically inactive mutant su...read more

Mentioned in this Paper

In Vivo NMR Spectroscopy
Amides
Alkalescens-Dispar Group
Extracellular
Calcium
Mutagenesis, Site-Directed
Myxobacter alpha-lytic proteinase
Subtilisins
Bacillus amyloliquefaciens
Fluorescence Spectroscopy
35

Related Papers

Paper Details
References
  • References23
  • Citations55
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