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Updated: Jun 15, 2026

Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
How conformational transition depends on hydrophobicity of elastin-like polypeptides
1Department of Physics Engineering, Ankara University, Dögol Caddesi 06100 Tandoğan, Ankara, Turkey. Handan.Olgar@eng.ankara.edu.tr
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.
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