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Electrostatic interactions in proteins
Sharp, K. A., International Tables for Crystallography (2012). Vol. F, ch. 22.4, pp. 730-735 [ doi:10.1107/97809553602060000888 ]
electrostatics – an optimal approach for large systems . J. Comput. Chem. 16, 898–913. Google Scholar Bruccoleri, R. E., Novotny, J., Sharp, K. A. & Davis, M. E. (1996). Finite difference Poisson–Boltzmann electrostatic calculations ...

Electrostatic contributions to binding energy
Sharp, K. A., International Tables for Crystallography (2012). Vol. F, Section 22.4.3.3, pp. 734-734 [ doi:10.1107/97809553602060000888 ]
Hecht, J., Sharp, K., Friedman, R. & Honig, B. (1994). Salt effects on protein–DNA interactions: the lambda cI repressor and Eco R1 endonuclease. J. Mol. Biol. 238, 264–280. Google Scholar Misra, V. & Honig, B. (1995 ...
     [more results from section 22.4.3 in volume F]

Calculation of energies and forces
Sharp, K. A., International Tables for Crystallography (2012). Vol. F, Section 22.4.2.4, pp. 732-732 [ doi:10.1107/97809553602060000888 ]
Reiner, E. S. & Radke, C. J. (1990). Variational approach to the electrostatic free energy in charged colloidal suspensions. J. Chem. Soc. Faraday Trans. 86, 3901. Google Scholar Sharp, K. & Honig, B. (1990). Calculating total ...
     [more results from section 22.4.2 in volume F]

Introduction
Sharp, K. A., International Tables for Crystallography (2012). Vol. F, Section 22.4.1, pp. 730-730 [ doi:10.1107/97809553602060000888 ]


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