Abstract
Raman and NMR spectroscopy together with DFT quantum chemical calculations have been used to elucidate conformational changes occurring during inverse temperature transition in water solution of two elastin-like polypentapeptides, poly(G1V1G2V2P) and poly(AV1GV2P). From the temperature dependences of Raman spectra and 1H–1H NOESY spectra follows that above the transition temperature a β(II)-turn conformational structure is formed on the residue located between Pro and Val1.