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Conformation of Synthetic Polypeptide Monolayers

Nature volume 231, pages 445–446 (1971)Cite this article

Abstract

PROTEINS and synthetic polypeptides spread at air/water interfaces are thought to exist in extended chain conformations1,2. From the results of deuterium exchange in monolayers, and infrared spectroscopy and electron diffraction on collapsed films, Malcolm3–5 reported that the α-helical conformation is stable in synthetic polypeptide monolayers. From the relationship between the temperature coefficient of monolayer transition pressure and the content of regular helix in the solid state, Yamashita and Yamashita6 reached a similar conclusion for poly-γ-benzyl glutamates.

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Author notes

  1. TAKUYA YAMASHITA

    Present address: Faculty of Pharmaceutical Sciences, University of Tokushima, Shomachi, Tokushima, 770

Authors and Affiliations

  1. Department of Chemistry, Faculty of Science, Osaka University, Toyonaka, Osaka, 560

    TAKUYA YAMASHITA

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  1. TAKUYA YAMASHITA
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YAMASHITA, T. Conformation of Synthetic Polypeptide Monolayers. Nature 231, 445–446 (1971). https://doi.org/10.1038/231445b0

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