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. 2013 Jun;44:31-9.
doi: 10.1016/j.compbiolchem.2013.02.005. Epub 2013 Mar 14.

Extending the Applicability of the O-ring Theory to protein-DNA Complexes


Extending the Applicability of the O-ring Theory to protein-DNA Complexes

R M Ramos et al. Comput Biol Chem. .


Many biological processes depend on protein-based interactions, which are governed by central regions with higher binding affinities, the hot-spots. The O-ring theory or the "Water Exclusion" hypothesis states that the more deeply buried central regions are surrounded by areas, the null-spots, whose role would be to shelter the hot-spots from the bulk solvent. Although this theory is well-established for protein-protein interfaces, its applicability to other protein interfaces remains unclear. Our goal was to verify its applicability to protein-DNA interfaces. We performed Molecular Dynamics simulations in explicit solvent of several protein-DNA complexes and measured a variety of solvent accessible surface area (SASA) features, as well as, radial distribution functions of hot-spots and null-spots. Our aim was to test the influence of water in their coordination sphere. Our results show that hot-spots tend to have fewer water molecules in their neighborhood when compared to null-spots, and higher values of ΔSASA, which confirms their occlusion from solvent. This study provides evidence in support of the O-ring theory with its applicability to a new type of protein-based interface: protein-DNA.

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