Protein-water hydrogen bonds are stabilized by electrostatic polarization

摘要

We study the dynamical properties of the hydration water around apo-myoglobin in this work under traditional AMBER force field and the polarized protein-specific charges (PPC). Both SPC/E and TIP3P water models are utilized in order to reveal the model dependence. With polarization effect taken into consideration as in the PPC, the hydrogen bonds between the protein and the solvation water molecules are strengthened. Therefore the lifetime of the hydrogen bonds increases, and both the rotational and translational motions of the water molecules are hindered. We also notice that these results have apparent model dependence, when comparing the SPC/E and TIP3P water models.View full textDownload full textKeywordselectrostatic polarization, hydration water, residence, rotational diffusion, Einstein diffusion constantRelated var addthis_config = { ui_cobrand: "Taylor & Francis Online", services_compact: "citeulike,netvibes,twitter,technorati,delicious,linkedin,facebook,stumbleupon,digg,google,more", pubid: "ra-4dff56cd6bb1830b" }; Add to shortlist Link Permalink http://dx.doi.org/10.1080/00268976.2012.668965