Holographic multiscale method used with non-biased atomistic forcefields for simulation of large transformations in protein

Abstract

We present a multiscale approach for simulating protein flexibility. The originality of our method is its ability to perform dynamic multiscaling based on continuous revaluation of overlapping areas. The holographic multiscale method overcomes the limitations of motions determined by predefined and fixed high-level descriptions and allows the reproduction of residue-specific impact on large scale motion. The method is tested with two different non-biased all atom implicit solvent forcefields. These show stretched proteins A and G, with maintained secondary structure, folding back near native states in a small number of transition events, demonstrating the advantages of this multiscale approach. © IOP Publishing Ltd.