Understanding the molecular basis of folding cooperativity through a comparative analysis of a multidomain protein and its isolated domains.

ABSTRACT: Although cooperativity is a well-established and general property of folding, our current understanding of this feature in multidomain folding is still relatively limited. In fact, there are contrasting results indicating that the constituent domains of a multidomain protein may either fold independently on each other or exhibit interdependent supradomain phenomena. To address this issue, here we present the comparative analysis of the folding of a tandem repeat protein, comprising two contiguous PDZ domains, in comparison to that of its isolated constituent domains. By analyzing in detail the equilibrium and kinetics of folding at different experimental conditions, we demonstrate that despite each of the PDZ domains in isolation being capable of independent folding, at variance with previ

SUBMITTER: Santorelli D 

PROVIDER: S-EPMC10017356 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature