Disulfide bonds in protein folding studies: friends or foes?
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.
Dadlez
M
M
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw.
D000818:Animals; D007611:Aprotinin / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D007768:Lactalbumin / Q000737:chemistry; D017510:Protein Folding
D004220:Disulfides; D007768:Lactalbumin; D007611:Aprotinin