Abstract
WE have found before that (Pro-Ala-Gly)n in the solid state has a slower hydrogen-deuterium exchange than (Pro-Gly-Ala)n which has almost the same molecular weight1. We think that this is caused by the higher stability of (Pro-Ala-Gly)n—(Pro-Gly-Ala)n does not build up such a stable form. Traub and Yonath2,3 have shown by X-ray diffraction that (Pro-Ala-Gly)n in the solid state is very similar to collagen. But although many experiments have been carried out recently4,5 it has not been possible to determine a structure of (Pro-Ala-Gly)n in solution. We have now succeeded in getting a high molecular weight product of (Pro-Ala-Gly)n, which shows a denaturation curve in solution similar to that of (Pro-Gly-Pro)n which was reported some time ago6.
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References
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HEIDEMANN, E., BERNHARDT, H. Synthetic Polypeptides as Models for Collagen. Nature 220, 1326–1327 (1968). https://doi.org/10.1038/2201326a0
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DOI: https://doi.org/10.1038/2201326a0
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