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
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.
© EDP Sciences, SIF, Springer-Verlag Berlin Heidelberg, 2010