Disulfide bonds in protein folding studies: friends or foes?

  • M Dadlez Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.;

Abstract

The studies on protein folding pathways utilizing disulfide bonds as reporter groups in several protein model systems are reviewed. Implications for a general mechanism of protein folding are discussed. An updated folding pathway for bovine pancreatic trypsin inhibitor (BPTI) based on recent data is proposed.
Published
1997-09-30
Section
Articles