Abstract
This review describes the progress of our recent studies on the conformation and the physical properties of amylose in solutions. In the first three sections, the equilibrium and dynamic aspects of the conformation are discussed in terms of the results obtained by hydrodynamic studies, computer modeling and fluorescence depolarization measurements. It was shown that the most reasonable model for the conformation is random coil having significant sequences of pseudohelical character. This model is compatible with the concept that the thermal segmental motion causes the imperfection of the helical structure and promotes a random-coil character of the amylose chain in solution. The following sections include two examples of the functional physical properties of amylose in aqueous solutions : the complex formation with a fluorescent dye and the retrogradation.
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