Unusual effects of an engineered disulfide on global and local protein stability.

doi:10.1021/bi9528558

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Article

Unusual effects of an engineered disulfide on global and local protein stability.

Biochemistry - 11 Jun 1996

Betz S F, Marmorino J L, Saunders A J, Doyle D F, Young G B, Pielak G J

Abstract excerpt

The global and local stabilities of a eukaryotic ferricytochrome c variant with an engineered disulfide are examined. The disulfide connects position 20, which is usually a valine, to position 102, which is usually a threonine. The cross-linked variant is approximately 1.2 kcal mol-1 less stable...

Topics

Amino Acid Sequence
Calorimetry
Circular Dichroism
Cytochrome c Group
Cytochromes c
Disulfides
Drug Stability
Genetic Variation
Magnetic Resonance Spectroscopy
Protein Conformation
Protein Engineering
Recombinant Proteins
Saccharomyces cerevisiae Proteins
Thermodynamics
Threonine

Source

Open in PubMed

Identifiers

PMID: 8652519
DOI: 10.1021/bi9528558

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8652519-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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