Human Frataxin Folds Via an Intermediate State. Role of the C-Terminal Region.

ABSTRACT: The aim of this study is to investigate the folding reaction of human frataxin, whose deficiency causes the neurodegenerative disease Friedreich's Ataxia (FRDA). The characterization of different conformational states would provide knowledge about how frataxin can be stabilized without altering its functionality. Wild-type human frataxin and a set of mutants, including two highly destabilized FRDA-associated variants were studied by urea-induced folding/unfolding in a rapid mixing device and followed by circular dichroism. The analysis clearly indicates the existence of an intermediate state (I) in the folding route with significant secondary structure content but relatively low compactness, compared with the native ensemble. However, at high NaCl concentrations I-state gains substantial c

SUBMITTER: Faraj SE 

PROVIDER: S-EPMC4746760 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature