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Article

Cysteine-free Rop: a four-helix bundle core mutant has wild-type stability and structure but dramatically different unfolding kinetics.

Protein science : a publication of the Protein Society - 1 Apr 2010

Hari Sanjay B, Byeon Chang, Lavinder Jason J, Magliery Thomas J

Abstract excerpt

Cysteine residues can complicate the folding and storage of proteins due to improper formation of disulfide bonds or oxidation of residues that are natively reduced. Wild-type Rop is a homodimeric four-helix bundle protein and an important model for protein design in the understanding of protein stability, structure and folding kinetics. In the native state, Rop has two buried, reduced cysteine residues in its...

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Identifiers

PMID: 20095056
DOI: 10.1002/pro.342
PMCID: PMC2867008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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