Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain.

Abstract excerpt

Incorrectly folded states transiently populated during the protein folding process are potentially prone to aggregation and have been implicated in a range of misfolding disorders that include Alzheimer's and Parkinson's diseases. Despite their importance, however, the structures of these states and the mechanism of their formation have largely escaped detailed characterization because of their short-lived...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Models, Molecular
• Share to Mutation