Studies of the collagen fold formation and gelation in solutions of a monodisperse α gelatin

Abstract

The reversion of a monodisperse α gelatin to the collagen fold over a concentration range up to 5 % w/v has been studied by n.m.r., dielectric relaxation, differential scanning calorimetry, optical rotation, viscometry and light scattering techniques. The folding process is shown to be intramolecular and the minimum concentration for gelling is correctly predicted from the behaviour of less concentrated solutions.