Isaac et. al (2015) studied the interaction between the flagellum of AMB-1 and different chirality CNTs (m-CNT and s-CNT). The observations through Molecular Dynamics simulations demonstrated that the glycine residues in D3 domain of flagellum interacts with m-CNT whereas such an interaction with s-CNT is absent. The specific interaction of glycine with m-CNT can lead to the development of a biological method for chirality based CNT sorting. Hence, further studies were required to determine the effect of the residues flanking glycine on it’s interaction with m-CNT. The type of interactions and the extent of interaction of different combinations of polar and non-polar amino acid residues flanking glycine were conducted. Hence, the role of glycine with two flanking amino acid residues (tripeptide) is substantiated to determine it’s specific interaction with m-CNT through the study of interaction energy and RMSD of the middle glycine and the flanking residues towards the adsorption of the tripeptide onto m-CNT
