Abstract
We have investigated the stability of backbone amide protons of the intermediate and the native state of the scFv fragment of an antibody. Stopped flow experiments analyzed by MS and NMR detected the formation of an exchange protected intermediate within the deadtime of the stopped flow apparatus (17 ms). H/D exchange rates of the native protein identified a number of very stable backbone amide protons in the V L and the V H domains. In the V L domain, this slowly exchanging core of the scFv fragment is similar to the folding core of the intermediate, while the V H domain possesses a great number of very stable amide protons which are not stabilized to a significant degree in the folding intermediate of the scFv fragment.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: 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.
