Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: equilibrium studies at neutral pH

Role of the disulphide bridge in folding

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

✍ Mariella Parisi; Alberto Mazzini; Robert Tibor Sorbi; Roberto Ramoni; Stefano Gr 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 239 KB

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 re