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Article

Role of the disulphide bridge in folding, stability and function of porcine odorant binding protein: spectroscopic equilibrium studies on C63A/C155A double mutant.

Biochimica et biophysica acta - 15 Jun 2005

Parisi Mariella, Mazzini Alberto, Tibor Sorbi Robert, Ramoni Roberto, Grolli Stefano, Favilla Roberto

Abstract excerpt

Porcine odorant binding protein (pOBP) contains a single disulphide bridge linking residues Cys63 and Cys155. In order to get information on the role played by this crosslink in determining the structural and functional properties of the protein, we substituted these two Cys residues with two Ala residues by site directed mutagenesis and investigated the changes in folding, stability and functional features, as...

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PMID: 15886077
DOI: 10.1016/j.bbapap.2005.04.003

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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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