How conformational transition depends on hydrophobicity of elastin-like polypeptides.
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.
Department of Physics Engineering, Ankara University, Dögol Caddesi 06100 Tandoğan, Ankara, Turkey. Handan.Olgar@eng.ankara.edu.tr
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D000595:Amino Acid Sequence; D004549:Elastin / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D009010:Monte Carlo Method; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D013696:Temperature; D013816:Thermodynamics
D009842:Oligopeptides; D004549:Elastin