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pKa values and redox potentials of proteins. What do they mean?

  • G. Matthias Ullmann EMAIL logo and Elisa Bombarda
Published/Copyright: January 28, 2013

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 pKa 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.


Corresponding author: G. Matthias Ullmann, Structural Biology/Bioinformatics, University of Bayreuth, Universitätsstrasse 30, BGI, 95447 Bayreuth, Germany

Received: 2012-11-17
Accepted: 2013-1-21
Published Online: 2013-01-28
Published in Print: 2013-05-01

©2013 by Walter de Gruyter Berlin Boston

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