Abstract
It is widely accepted that the folding process of a protein is in large part determined by topology of the native structure. A class of coarse-grained model called Go-like model that takes only the native-state topology into account has successfully described folding of many proteins. In this letter, we show that a Go-like model with reduced number of amino acids exhibits a similar free-energy landscape for Ribonuclease H to one obtained by Go-like model. Coarser-grained Go-like model shows a qualitatively same variation of the free-energy landscape due to energy balance between domains.
