Gross, P.C.P.C.GrossPossart, W.W.PossartZeppezauer, M.M.Zeppezauer2022-03-032022-03-032003https://publica.fraunhofer.de/handle/publica/203353Polypentapeptides (GVGVP)(n) which are designed in analogy to the connective tissue protein elastin are reported to transform various kinds of energy into mechanical work by the so-called DeltaT(t)-mechanism in cross-linked macroscopic polypentapeptide (PPP) films. In the literature, the responsible element of conformation in such polypeptides is described as a beta-spiral and the DeltaT(t) effect is explained as a sudden change of macroconformation of single polypeptide molecules from an extended but not regular state below a transition temperature T-t to the beta-spiral above T-t. We examined the secondary structure of the linear PPP C(GVGVP)(6) in solution with DSC, CD, UV absorption, FTIR and NMR spectroscopy. The results suggest that the beta-spiral is not present in the conformational structure of the PPP molecules. The antiparallel beta-sheet is proposed to be the basic regular part of conformation because it agrees with all spectroscopic data. As a consequence, the elasticity of natural elastin must be considered from a new perspective.en620660671669journal article