Abstract
In relation to denaturation of proteins, thermally induced conformational change of poly(D-glutamic acid) was studied in the presence of poly(vinyl alcohol) at low pH, where poly(D-glutamic acid) undergoes a helix-to-${\beta}$ transition without any other polymer. In a dilute solution, poly(vinyl alcohol) enhanced the ${\alpah}-to-{\beta}_1$ transition of poly(D-glutamic acid) due to intermolecular interaction between the two polymers. On the other hand, this conformational change was interrupted to a large extent in a concentrated solution, due to the interpenetration of poly(vinyl alcohol) chain into poly(D-glutamic acid) chain which prevented the intramolecular association of poly(D-glutamic acid) chain. A conformational change from ${\beta}_1\;to\;{\beta}_2$ of poly(D-glutamic acid) was observed for the films obtained by casting during annealing the mixture solutions. The ${\beta}_2$ content in the cast film increased with increasing poly(vinyl alcohol) content in the mixture.