Eur. Phys. J. E (2010) 31: 327-332
https://doi.org/10.1140/epje/i2010-10573-7

Regular Article

How conformational transition depends on hydrophobicity of elastin-like polypeptides

Department of Physics Engineering, Ankara University, Dögol Caddesi 06100 Tandoğan, Ankara, Turkey

^* e-mail: Handan.Olgar@eng.ankara.edu.tr

Received: 12 May 2009
Revised: 19 January 2010
Accepted: 27 January 2010
Published online: 13 March 2010

Abstract

The three-dimensional structures of elastin-like polypeptides Val1-Pro2-Gly3-Xaa4-Gly5 were investigated by using the multicanonical Monte Carlo (MC) simulation procedure. By substituting different amino acids in the fourth position of the sequence, the thermodynamical variables are calculated in vacuo and in solvent to determine the hydrophobicity dependence of the conformational transition temperatures of the peptides. Resultant hydrophobicity scale is in good agreement with many hydrophobicity scales.