The ability to represent accurately interactions between biomolecular assemblies at the atomic level is required for computational simulations in important areas such as drug optimisation and enzyme catalysis. Usually such simulations are performed by empirical classical force fields or with hybrid quantum/classical (QM/MM) approaches. A new and exciting possibility for obtaining biomolecular interactions is offered by the ONETEP linear-scaling density functional theory (DFT) program [1], with which we can perform large-scale DFT calculations with near-complete basis set accuracy. This approach naturally overcomes the transferability issues of empirical force fields as well as the arbitrariness of QM/MM interfaces, but appropriate schemes for configurational sampling [2] need to be developed as well as schemes for treating the solvent [3]. We present calculations of hydration free energies and protein-ligand free energies of binding obtained by DFT calculations on entire proteins with thousands of atoms. References [1] C.-K. Skylaris, P. D. Haynes, A. A. Mostofi and M. C. Payne. J. Chem. Phys. 122 , 084119  (2005).[2] F. R. Beierlein, J. Michel, and J. W. Essex, J. Phys. Chem. B 115 , 4911 (2011); D. J. Cole, C.-K. Skylaris, E. Rajendra, A. R. Venkitaraman and M. C. Payne. Europhysics Letters 91 , 37004 (2010); S. Fox, H. Wallnoefer, T. Fox, C. Tautermann , and C.-K. Skylaris. J. Chem. Theor. Comput. 7 , 1102 (2011).[3] J. Dziedzic, H. H. Helal, C.-K. Skylaris, A. A. Mostofi, and M. C. Payne. Europhysics Letters 95 , 43001 (2011); S. Fox, C. Pittock, T. Fox, C. Tautermann, Noj Malcolm, and C.-K. Skylaris. To appear in J. Chem. Phys.

Biomolecular interactions from linear-scaling density functional theory calculations with thousands of atoms

243rd National Meeting (2012)

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