Abstract
The promotion of protein folding is an important subject that can contribute to the efficient production of biological medicines. Here we report the promotion of disulfide bond-coupled protein folding by imidazoyl-conjugated thiol (ImdSH). ImdSH accelerated the disulfide bond formation and folding of reduced ribonuclease A and bovine pancreatic trypsin inhibitor relative to glutathione as a conventionally used additive.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.