Assessing The Heme Group Interactions Of Hemoglobin And Myoglobin In Deoxy And Oxy Form

Heme proteins such as hemoglobin and myoglobin’s role are primarily associated to binding molecular oxygen for proper functioning. Heme moiety in both these proteins is found to be incorporated in a hydrophobic cleft and is responsible for oxygen binding. The interactions of amino acids surrounding heme group support in ligand binding and contribute to protein’s functionality. Moreover, nano-ligands, drugs and dyes may bind near heme involving the nearby residues and accordingly those residues possibly take part in regulating the overall functionality of these proteins. Hence, studying the heme group interactions with neighbouring residues will unravel contribution of these residues in determining structural functionality of the proteins. Apparently, this work focuses on identifying the key residues and the nature of interactions surrounding heme of hemoglobin and myoglobin in deoxy and oxy form. These residues can be used to design and engineer novel peptide molecules of clinical significance. Our study also highlights contribution of specific Tyr/ Trp molecules in heme group interactions suggesting their roles not only in binding interactions but also in the development of fluorescence-based protein sensors and bio-imaging.