Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V.

doi:10.1110/ps.26801

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Article

Disulfide bond effects on protein stability: designed variants of Cucurbita maxima trypsin inhibitor-V.

Protein science : a publication of the Protein Society - 1 Jan 2001

Zavodszky M, Chen C W, Huang J K, Zolkiewski M, Wen L, Krishnamoorthi R

Abstract excerpt

Attempts to increase protein stability by insertion of novel disulfide bonds have not always been successful. According to the two current models, cross-links enhance stability mainly through denatured state effects. We have investigated the effects of removal and addition of disulfide cross-links, protein flexibility in the vicinity of a cross-link, and disulfide loop size on the stability of Cucurbita maxima...

Topics

Circular Dichroism
Cross-Linking Reagents
Cucurbitaceae
Disulfides
Hydrogen Bonding
Mutation
Plant Proteins
Protein Denaturation
Protein Engineering
Protein Folding
Thermodynamics

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PMID: 11266603
DOI: 10.1110/ps.26801
PMCID: PMC2249841

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