Simulations of elastin like proteins

(VPGXG)_n polypeptides known as elastin-like polypeptides with different biological, biomechanical, biochemical and biophysical properties stand out suitable structures appropriate for production of several biomaterials, in the first instance, tissue, microtube and nanotube in tissue engineering. Therefore, understanding the structural properties of such peptides comes into prominence. For this purpose, structural properties of elastin-like polypeptides have been investigated by computer simulation methods in our study. Our simulations have been carried out by multicanonical algorithm having a wide range of application area from solid state to biophysics, the most powerful algorithm in generalized ensemble family. By taking n=1 and changing aminoacid X, hydrophobicity scale has been established in the forepart of our study, afterwards the effect on structural transition temperature has been determined in a solvent (SCH2) and vacuum. In the second part, choosing VPGVG, the most repeating pentapeptide sequence in elastin-like proteins, and taking n=1, 2, 3, 4, change in structural transition temperature and secondary structure formation caused by the transition from smaller molecule to larger one have been determined.