Folding disulfide-containing proteins faster with an aromatic thiol
JD Gough, RH Williams, AE Donofrio…
文献索引：Gough, Jonathan D.; Williams Jr., Rhondye H.; Donofrio, Anthony E.; Lees, Watson J. Journal of the American Chemical Society, 2002 , vol. 124, # 15 p. 3885 - 3892
The traditional method for in vitro folding of disulfide-containing proteins is slow and involves a redox buffer of glutathione and glutathione disulfide. To increase the folding rate and to gain insight into the folding process, we replaced glutathione, an aliphatic thiol, with a commercially available aromatic thiol, 4-mercaptobenzeneacetate (1). Aromatic thiol 1 was selected due to its enhanced nucleophilicity and its enhanced leaving-group ability ...
