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Article

DSC studies of the conformational stability of barstar wild-type.

Protein science : a publication of the Protein Society - 1 Oct 1997

Schöppe A, Hinz H J, Agashe V R, Ramachandran S, Udgaonkar J B

Abstract excerpt

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 shown by a ratio of delta HvH/delta Hcal near 1 that denaturation follows a two-state mechanism. For comparison, the C82A mutant...

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Identifiers

PMID: 9336842
DOI: 10.1002/pro.5560061014
PMCID: PMC2143573

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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