Recent advances in helix-coil theory

    Research output: Contribution to journalArticlepeer-review


    Peptide helices in solution form a complex mixture of all helix, all coil or, most frequently, central helices with frayed coil ends. In order to interpret experiments on helical peptides and make theoretical predictions on helices, it is therefore essential to use a helix-coil theory that takes account of this equilibrium. The original Zimm-Bragg and Lifson-Roig helix-coil theories have been greatly extended in the last 10 years to include additional interactions. These include preferences for the N-cap, N1, N2, N3 and C-cap positions, capping motifs, helix dipoles, side chain interactions and 310-helix formation. These have been applied to determine energies for these preferences from experimental data and to predict the helix contents of peptides. This review discusses these newly recognised structural features of helices and how they have been included in helix-coil models. © 2002 Elsevier Science B.V. All rights reserved.
    Original languageEnglish
    Pages (from-to)281-293
    Number of pages12
    JournalBiophysical Chemistry
    Publication statusPublished - 10 Dec 2002


    • α-Helix
    • Lifson-Roig
    • Protein stability
    • Protein structure
    • Random coil
    • Zimm-Bragg


    Dive into the research topics of 'Recent advances in helix-coil theory'. Together they form a unique fingerprint.

    Cite this