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Proteins change their charge state through protonation and redox reactions aswell as through binding charged ligands. The free energy of these reactions aredominated by solvation and electrostatic energies and modulated by proteinconformational relaxation in response to the ionization state changes. Althoughcomputational methods for calculating these interactions can provide verypowerful tools for predicting protein charge states, they include severalcritical approximations of which users should be aware. This chapter discussesthe strengths, weaknesses, and approximations of popular computational methodsfor predicting charge states and understanding their underlying electrostaticinteractions. The goal of this chapter is to inform users about applicationsand potential caveats of these methods as well as outline directions for futuretheoretical and computational research.

Continuum Electrostatics Approaches to Calculating p$K_a$s and $E_m$s in Proteins