@article {101471,
	title = {Energetics of protein{\textendash}DNA interactions},
	journal = {Nucl. Acids Res.},
	volume = {35},
	year = {2007},
	month = {2007},
	pages = {1039 - 1047},
	abstract = {Protein{\textendash}DNA interactions are vital for many processes in living cells, especially transcriptional regulation and DNA modification. To further our understanding of these important processes on the microscopic level, it is necessary that theoretical models describe the macromolecular interaction energetics accurately. While several methods have been proposed, there has not been a careful comparison of how well the different methods are able to predict biologically important quantities such as the correct DNA binding sequence, total binding free energy and free energy changes caused by DNA mutation. In addition to carrying out the comparison, we present two important theoretical models developed initially in protein folding that have not yet been tried on protein{\textendash}DNA interactions. In the process, we find that the results of these knowledge-based potentials show a strong dependence on the interaction distance and the derivation method. Finally, we present a knowledge-based potential that gives comparable or superior results to the best of the other methods, including the molecular mechanics force field AMBER99.},
	url = {http://dx.doi.org/10.1093/nar/gkl1103},
	author = {Donald, Jason E. and Chen, William W. and Eugene I. Shakhnovich}
}
