Executive Summary : | Proteins are a defined sequence of amino acids which are essential for the regulation of biological processes. The functional properties of proteins are almost endless. Their functionalities are evident in signalling pathway, RNA trans phosphorylation, regulation of cell cycle, DNA repair, and transcription via signal transduction to name a few. Importance of studying proteins is inevitable as proteins unleashes their potential in various application including drug delivery and cancer treatment. In most of the scenarios, the functionality of a peptide is determined by the primary and the secondary structure. In few cases the activity also depends on the interactions with other proteins or peptides. The understanding of protein-peptide interactions has been an interesting area of research. An example for protein-peptide interaction driven activity is the classic case of RNase-S. RNase-S belongs to the family of Ribonuclease and these are the proteins which catalyze the degradation of RNA. RNase-A is specific to single-stranded RNAs, while RNase-S is a derivative of RNase-A and it catalyzes both the trans phosphorylation of RNA to form a 2,3-cyclic phosphodiester intermediate and hydrolysis of this cyclic intermediate to form a 3-phosphomonoester. It is important to understand the structural and conformational details of RNase-S in order to understand its catalytic activity and mechanism of action. The interaction between the S-protein and S-peptide can also be used as a model to study other similar protein-peptide binding mechanism. |