Importance of Long-Range Interactions for Determining the Folding Rate and Transition State Structures of Two-state Proteins

Elucidating the mechanism of protein folding is an intriguing and challenging task. Currently, tremendous advances have been explored and the combination of experimental and theoretical approaches provides new insights to protein folding [3]. The formation of stable secondary structures and a unique tertiary structure of a protein is mainly dictated by interactions between amino acid residues along the polypeptide chain. Consequently, medium and long-range interactions play an active role in the folding and stability of proteins. In this article, we discuss about the development of a novel parameter, long-range order (LRO) and its application for predicting the protein folding rates of two-state proteins. Further, we revealed the important amino acid properties for determining the transition state structures of two-state protein mutants.