Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

Advertisement

Polymer Journal
  • View all journals
  • Search
  • Log in
  • Content Explore content
  • About the journal
  • Publish with us
  • Sign up for alerts
  • RSS feed
  1. nature
  2. polymer journal
  3. regular article
  4. article
X-Ray Structural Studies of Some Poly(α-amino acid)s with Hydrophobic Side Chains: Poly(L-valine), Poly(L-isoleucine), and Poly(L-phenylalanine)
Download PDF
Download PDF
  • Regular Article
  • Published: 01 October 1979

X-Ray Structural Studies of Some Poly(α-amino acid)s with Hydrophobic Side Chains: Poly(L-valine), Poly(L-isoleucine), and Poly(L-phenylalanine)

  • Osamu Yamashita1,
  • Takashi Yamane1,
  • Tamaichi Ashida1,
  • Shinsuke Yamashita2 &
  • …
  • Takuya Yamashita2 

Polymer Journal volume 11, pages 763–774 (1979)Cite this article

  • 1421 Accesses

  • 19 Citations

  • Metrics details

Abstract

X-Ray structure studies of poly(L-valine), poly(L-isoleucine), and poly(L-phenylalanine) have been carried out. Poly(L-valine) has two structural forms. One is an α-helical conformation packed in the hexagonal lattice with a dimension of a=11.43 Å, though this conformation is unfavorable for poly(L-valine). The other is a β pleated sheet structure with the crystal data: P212121, a=4.80 Å, b=19.14 Å, c=6.59 Å (fiber axis). The β poly(L-valine) gave an X-ray fiber photograph of high quality and a detailed structural study was carried out. Poly(L-isoleucine) also crystallizes in a β pleated sheet structure with a=4.8 Å, b=23 Å, c=6.6 Å, orthorhombic. Contraction of fiber axes in both β structures are observed. The X-ray fiber photograph of poly(L-phenylalanine) suggests the coexistence of ω- and α-helix. This specimen may be the third example of an ω-helix. The significance of the hydrophobic interaction of the side chains in the structures is discussed.

Similar content being viewed by others

Allosteric amyloid catalysis by coiled coil fibrils

Article Open access 31 May 2025

Ring-opening polymerization of six-membered cyclic hybrid dimers composed of an oxoester and thioester

Article Open access 15 May 2024

Single crystals of mechanically entwined helical covalent polymers

Article 03 May 2021

Article PDF

References

  1. S. Arnott, S. D. Dover, and A. Elliott, J. Mol. Biol., 30, 201 (1967).

  2. V. Sasisekharan, Acta Crystallogr., 12, 897 (1959).

  3. S. Yamashita and T. Yamashita, Proc. Natl. Acad. Sci., U.S.A., 72, 941 (1975).

  4. E. R. Blout, C. De Lozé, S. M. Bloom, and G. D. Fasman, J. Am. Chem. Soc., 82, 3787 (1960).

  5. S. Arnott, Polymer, 6, 478 (1965).

  6. S. Arnott and A. J. Wonacott, J. Mol. Biol., 21, 371 (1966).

  7. C. H. Bamford, W. E. Hanby, and F. Happey, Proc. R. Soc. London, Ser. A, 205, 30 (1951).

  8. L. Brown and I. F. Trotter, Trans. Faraday Soc., 52, 537 (1956).

  9. L. Pauling and R. B. Corey, Proc. Natl. Acad. Sci., U.S.A., 39, 253 (1953).

  10. T. Miyazawa, J. Polym. Sci., 55, 215 (1961).

  11. E. M. Bradbury, L. Brown, A. R. Downie, A. Elliott, W. E. Hanby, and T. R. R. McDonald, Nature, 183, 1736 (1959).

  12. E. M. Bradbury, L. Brown, A. R. Downie, A. Elliott, R. D. B. Fraser, and W. E. Hanby, J. Mol. Biol., 5, 230 (1962).

  13. R. D. B. Fraser, T. P. MacRae, and I. W. Stapleton, Nature, 193, 573 (1962).

  14. S. Yamashita and T. Yamashita, to be published.

Download references

Author information

Authors and Affiliations

  1. Department of Applied Chemistry, Faculty of Engineering, Nagoya University,

    Osamu Yamashita, Takashi Yamane & Tamaichi Ashida

  2. Faculty of Pharmaceutical Sciences, Tokushima University,

    Shinsuke Yamashita & Takuya Yamashita

Authors
  1. Osamu Yamashita
    View author publications

    Search author on:PubMed Google Scholar

  2. Takashi Yamane
    View author publications

    Search author on:PubMed Google Scholar

  3. Tamaichi Ashida
    View author publications

    Search author on:PubMed Google Scholar

  4. Shinsuke Yamashita
    View author publications

    Search author on:PubMed Google Scholar

  5. Takuya Yamashita
    View author publications

    Search author on:PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yamashita, O., Yamane, T., Ashida, T. et al. X-Ray Structural Studies of Some Poly(α-amino acid)s with Hydrophobic Side Chains: Poly(L-valine), Poly(L-isoleucine), and Poly(L-phenylalanine). Polym J 11, 763–774 (1979). https://doi.org/10.1295/polymj.11.763

Download citation

  • Issue date: 01 October 1979

  • DOI: https://doi.org/10.1295/polymj.11.763

Share this article

Anyone you share the following link with will be able to read this content:

Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative

Keywords

  • Poly(L-valine)
  • Poly(L-isoleucine)
  • Poly(L-phenylalanine)
  • α-Helix
  • ω-Helix
  • β Pleated Sheet
  • X-Ray Diffraction
  • Hydrophobic Interaction
Download PDF

Advertisement

Explore content

  • Research articles
  • Reviews & Analysis
  • News & Comment
  • Current issue
  • Collections
  • Follow us on Twitter
  • Sign up for alerts
  • RSS feed

About the journal

  • Journal Information
  • Open Access Fees and Funding
  • About the Editors
  • Contact
  • About the Partner
  • For Advertisers
  • Subscribe
  • Featured Articles

Publish with us

  • For Authors & Referees
  • Language editing services
  • Open access funding
  • Submit manuscript

Search

Advanced search

Quick links

  • Explore articles by subject
  • Find a job
  • Guide to authors
  • Editorial policies

Polymer Journal (Polym J)

ISSN 1349-0540 (online)

ISSN 0032-3896 (print)

nature.com sitemap

About Nature Portfolio

  • About us
  • Press releases
  • Press office
  • Contact us

Discover content

  • Journals A-Z
  • Articles by subject
  • protocols.io
  • Nature Index

Publishing policies

  • Nature portfolio policies
  • Open access

Author & Researcher services

  • Reprints & permissions
  • Research data
  • Language editing
  • Scientific editing
  • Nature Masterclasses
  • Research Solutions

Libraries & institutions

  • Librarian service & tools
  • Librarian portal
  • Open research
  • Recommend to library

Advertising & partnerships

  • Advertising
  • Partnerships & Services
  • Media kits
  • Branded content

Professional development

  • Nature Awards
  • Nature Careers
  • Nature Conferences

Regional websites

  • Nature Africa
  • Nature China
  • Nature India
  • Nature Japan
  • Nature Middle East
  • Privacy Policy
  • Use of cookies
  • Legal notice
  • Accessibility statement
  • Terms & Conditions
  • Your US state privacy rights
Springer Nature

© 2026 Springer Nature Limited