期刊
EPL
卷 91, 期 3, 页码 -出版社
IOP PUBLISHING LTD
DOI: 10.1209/0295-5075/91/37004
关键词
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资金
- EPSRC [EP/F032773/1]
- University of Southampton
- Royal Society for a University Research Fellowship
- UK Medical Research Council
- EPSRC [EP/F032773/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/F032773/1] Funding Source: researchfish
A modification of the MM-PBSA technique for calculating binding affinities of biomolecular complexes is presented. Classical molecular dynamics is used to explore the motion of the extended interface between two peptides derived from the BRC4 repeat of BRCA2 and the eukaryotic recombinase RAD51. The resulting trajectory is sampled using the linear-scaling density functional theory code, ONETEP, to determine from first principles, and with high computational efficiency, the relative free energies of binding of the similar to 2800 atom receptor-ligand complexes. This new method provides the basis for computational interrogation of protein-protein and protein-ligand interactions within fields ranging from chemical biological studies to small-molecule binding behaviour, with both unprecedented chemical accuracy and affordable computational expense. Copyright (c) EPLA, 2010
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