Abstract
AbstractTo investigate the flexibility or motility of the secondary structure of poly‐L‐glutamic acid, a simple model molecule of proteins, the kinetics of the tritium–hydrogen exchange of this polymer in aqueous solutions was followed at various pH values by use of a freeze‐drying technique and a liquid scintillation counter. The most essential point of the experimental results is that all of the protons (or isotopes) attached to peptide nitrogens were exchanged according to a simple first‐order reaction and the rate was proportional to the fraction of random coil conformation determined by optical rotatory dispersion measurements. This means that the tritium attached to a peptide unit is exchangeable with a proton in water only when this unit is contained in the random coil structure and that the interchange of each unit between helical and random coil conformations takes place as a result of thermal fluctuation at very high frequency, although the average helical content of each molecule has a definite value.
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.
