抄録
During the process of protein folding, the amino acid residues along the polypeptide chain interact with each other in a cooperative manner to form the stable native structure. The knowledge about interactions between amino acid residues in protein structures is very helpful to understand the mechanism of protein folding and stability. In this review, I classify the inter-residue interactions into short, medium and long range based on a simple geometric approach. The features of these interactions in different structural classes and folding types of globular proteins have been delineated. Further, the development of a new parameter, long-range order, based on inter-residue interactions and its application for predicting the protein folding rates are highlighted. The information gained from the studies on inter-residue interactions provides valuable insights for understanding protein folding and de novo protein design.
