✍ Scribed by Ginka S. Buchner; Ronan D. Murphy; Nicolae-Viorel Buchete; Jan Kubelka
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
This study focuses on the phenomenon of kinetic partitioning when a polypeptide chain has two ground-state conformations, one of which is kinetically more reachable than the other. We designed sequences for lattice model proteins with two different conformations of equal energy corresponding to the
## Abstract A method of calculating time correlation functions from records of computer simulated equilibrium conformational fluctuations in a globular protein is discussed. Use of the calculated time correlation function for discussions of dynamics of folding and unfolding transition in the two‐di
The kinetics of the hydrodynamic volume change associated with the unfolding and refolding of a globular protein can be observed using high performance size exclusion chromatography. Chromatographic profiles that evidence such dynamics can be simulated using equations in which chromatographic partit