PROTEIN-FOLDING COUPLED TO DISULFIDE BOND FORMATION

Protein folding that is coupled to disulphide bond formation has many experimental advantages. In particular, the kinetic roles and importan ce of all the disulphide intermediates can be determined, usually unam biguously. This contrasts with other types of protein folding, where t he roles of any intermediates detected are usually not established. Ne vertheless, there is considerable confusion in the literature about ev en the best-characterized disulphide folding pathways. This article at tempts to set the record straight.