Abstract
Light-scattering measurements were carried out on fractions of poly-N5-(3-hydroxypropyl)-L-glutamine (PHPG) in mixtures of methanol and water over ranges of temperature and solvent composition which covered the entire course of a helix–coil transition. Data for the mean-square radii of gyration ‹S2› were determined as a function of the parameters N, u, and σ basic to the theories of the helix–coil transition of polypeptides, where N is the number of monomeric units, u the equilibrium constant for helix formation, and σ the helix-initiation parameter. The data were analyzed in terms of the procedure proposed recently by Teramoto, et al., and it is shown that the molecular chain in the transition region could well be represented by an alternating sequence of helical sections characterized by a pitch of 1.65±0.05Å and randomly coiled sections represented by random flight chains with a step length of 15±0.5Å. The value of 1.65Å is favorably compared to that for the α-helix. These results lend support to the theory of Nagai for ‹S2› and its subsequent extensions.
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Okita, K., Teramoto, A. & Fujita, H. Solution Properties of Synthetic Polypeptides. IX. Light-Scattering Study of Poly-N5-(3-hydroxypropyl)-L-glutamine in the Helix–Coil Transition Region. Polym J 1, 582–590 (1970). https://doi.org/10.1295/polymj.1.582
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DOI: https://doi.org/10.1295/polymj.1.582
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