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Structure and Stability of the α-Helix

Lessons for Design

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Protein Design

Part of the book series: Methods in Molecular Biology ((MIMB,volume 340))

Abstract

The α-helix is the most abundant secondary structure in proteins. We now have an excellent understanding of the rules for helix formation because of experimental studies of helices in isolated peptides and within proteins, examination of helices in crystal structures, computer modeling and simulations, and theoretical work. Here we discuss structural features that are important for designing peptide helices, including amino acid preferences for interior and terminal positions, side chain interactions, disulfide bonding, metal binding, and phosphorylation. The solubility and stability of a potential design can be predicted with helical wheels and helix/coil theory, respectively. The helical content of a peptide is most often quantified by circular dichroism, so its use is discussed in detail.

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Authors and Affiliations

  1. Faculty of Life Sciences, The University of Manchester, Manchester, UK

    Neil Errington & Andrew J. Doig

  2. Faculty of Life Sciences, Jackson’s Mill, The University of Manchester, Manchester, UK

    Teuku Iqbalsyah

Authors
  1. Neil Errington
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  2. Teuku Iqbalsyah
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  3. Andrew J. Doig
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Editor information

Editors and Affiliations

  1. Département de Biologie Joliot–Curie CEA Saclay, Gif-sur-Yvette, France

    Raphael Guerois

  2. Merz Pharmaceuticals GmbH, Frankfurt am Main, Germany

    Manuela López de la Paz

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© 2006 Humana Press Inc.

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Errington, N., Iqbalsyah, T., Doig, A.J. (2006). Structure and Stability of the α-Helix. In: Guerois, R., de la Paz, M.L. (eds) Protein Design. Methods in Molecular Biology, vol 340. Humana Press. https://doi.org/10.1385/1-59745-116-9:3

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  • DOI: https://doi.org/10.1385/1-59745-116-9:3

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-585-9

  • Online ISBN: 978-1-59745-116-1

  • eBook Packages: Springer Protocols

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