Publication

Abstract : Molecular motors can be considered as biological molecular devices that are indispensable agents or machines for movement in living organisms. The most common motor proteins are Myosin, Kinesin and Dynein which are responsible for nanoscale cellular and molecular movement. In this work, the above mentioned protein molecules have been subjected to structural and sequence analysis, modeling and molecular dynamics simulation to study their properties and control aspects. Structural and sequence studies, interactional analysis and thermodynamic characterization effectively support the possibility for designing of biomolecular systems with these molecular motors as the source of driving force. Most of these protein molecules are found to be thermodynamically stable keeping active sites for interaction with ligands. It was also found that most of the protein molecules from the kinesin family possessed an appreciably high stability even after the temperature evolution of the molecule. This suggests the possibility for designing kinesin-based biomolecular systems.