Abstract
The helix–coil transition kinetics of two 14-residue helical peptides of different stability were studied by time-resolved infrared (IR) spectroscopy coupled with laser-induced temperature-jump (T-jump) technique. The T-jump induced relaxation kinetics of both peptides show strong dependence on the final temperature, implying the existence of an enthalpic barrier for the nucleation process. In addition, the peptide with end-capping groups, which is more stable, folds faster. Together, these results suggest that the overall helical stability plays an important role in controlling the kinetics of the helix–coil transition, in agreement with results of early theoretical studies.
Sign-in/Register to access full text options 
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.
