Chapter 22.4 Electrostatic interactions in proteins
Crystallography of biological macromolecules
Second Online Edition (2012)
Part 22. Molecular geometry and features
Published Online: 14 APR 2012
© International Union of Crystallography 2006
International Tables for Crystallography
How to Cite
Sharp, K. A. 2012. Electrostatic interactions in proteins. International Tables for Crystallography. F:22:22.4:730–735.
- Published Online: 14 APR 2012
Electrostatic interactions play a key role in determining the structure, stability, binding affinity and chemical properties, and hence the biological reactivity, of proteins and nucleic acids. The goal of electrostatic calculations is to take the structural information provided by crystallography or NMR and obtain a realistic description of the electrostatic potential distribution ϕ(r), energies and forces. Three problems must be solved to obtain the electrostatic potential distribution: modelling the macromolecular charge distribution; modelling the response of the macromolecule, water and solvent ions; and rapidly and accurately solving the electrostatic equations that determine the potential. The response arises from electronic polarization, reorientation of permanent dipolar groups and redistribution of mobile ions in the solvent. The most common theoretical approaches to modelling this response are briefly described, along with the methods used to obtain potential distributions, energies and forces. A summary of the theory behind application to three broad areas is presented: electrostatic potential distributions, charge (proton and electron) transfer equilibria, and electrostatic contributions to binding energies.
- binding energies;
- charge‐transfer equilibria;
- electrostatic fields;
- electrostatic interactions in proteins;
- electrostatic potential;