Abstract
In this article, we review a microstate model that uses protonation and redox microstates in order to understand the complex pH and redox titration of proteins and other polyelectrolytes. From this model, it becomes obvious that it is impossible to assign pK(a) values or redox potentials to individual protonatable or redox-active sites in a protein in which many of such sites interact. Instead each site is associated with many microscopic equilibrium constants that may lead to irregular or even non-monotonic titration curves of some groups. The microstate model provides a closed theoretical framework to discuss such phenomena.
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.
