Abstract
The ubiquitous nature of the helical fold and its characteristic physical properties make it one of the first candidates for studies of secondary structure formation in polypeptides, and the thermodynamics of helix formation is a common topic in many classical biophysics textbooks. However, though there is general agreement on the features of the equilibrium properties of the coil-to-helix transition, both experimental and theoretical studies have provided widely varying estimates of helix formation rates from tens of picoseconds to microseconds. We present results of recent molecular simulations of several helix-forming peptides that permit the quantitative study of both intra- and inter-helical contacts in polypeptides. This analysis of local, site-specific formation of intra- and inter-chain interactions is necessary for any quantitative modeling of the elementary steps of secondary and tertiary structure formation in protein folding, and it allows direct comparison to data from recent infrared vibrational spectroscopy studies.
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.
