Hydrodynamic Interactions in Protein Folding

We incorporate hydrodynamic interactions (HI) in a coarse-grained and structure-based model of proteins by employing the Rotne-Prager hydrodynamic tensor. We study several small proteins and demonstrate that HI facilitate folding. We also study HIV-1 protease and show that HI make the flap closing dynamics faster. The HI are found to affect time correlation functions in the vicinity of the native state even though they have no impact on same time characteristics of the structure fluctuations around the native state

Stretching and twisting of the DNA duplexes in coarse grained dynamical models

Three coarse-grained models of the double-stranded DNA are proposed and compared in the context of mechanical manipulation such as twisting and various schemes of stretching. The models differ in the number of effective beads (between two and five) representing each nucleotide. They all show similar behavior and, in particular, lead to a torque-force phase diagrams qualitatively consistent with experiments and all-atom simulations