Protein simulations combining an all-atom force field with a Go term

TL;DR

This paper explores how coupling an all-atom protein force field with a Go-like potential influences sampling, revealing that the native structure can be stabilized as the global minimum through this combined approach.

Contribution

It introduces a method combining all-atom force fields with a Go-term to better stabilize native protein structures in simulations.

Findings

Adding a Go-term deforms the energy landscape

Native structure becomes the global minimum with the Go-term

Native is not the lowest-energy in pure all-atom models

Abstract

Using a variant of parallel tempering, we study the changes in sampling within a simulation when the all-atom model is coupled to a Go-like potential. We find that the native structure is not the lowest-energy configuration in the all-atom force field. Adding a Go-term deforms the energy landscape in a way that the native configuration becomes the global minimum.