BAROMECHANICAL TRANSDUCTION IN A MODEL PROTEIN BY THE DELTA-T(T) MECHANISM

Polypeptides of the composition poly[f(V)(GVGVP),f(X)(GXGVP)] exhibit inverse temperature transitions wherein there is an increase in order due to hydrophobic folding and assembly on raising the temperature. In cross-linked matrices, the transition is observed as a thermally-driven contraction capable of performing mechanical work, that is, as thermomechanical transduction. The temperature, T(t), at which the inverse temperature transition occurs, is dependent on pressure when X is an aromatic, Phe (F), residue. For cross-linked matrices of poly[0.79(GVGVP), 0.21(GFGVP)], it is reported here that the temperature at which thermomechanical transduction occurs increases on increasing the pressure, and that release of pressure results in contraction with the lifting of a weight. Thus baromechanical transduction in a model protein system is demonstrated.