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Structural analysis of alpha-helical proteins from wool using cysteine labelling and mass spectrometry

  • R. D M O'Cualain
  • , P. F G Sims
  • , C. M. Carr

    Research output: Contribution to journalArticlepeer-review

    Abstract

    A simple reduction/labelling/extraction protocol has been developed to fractionate cortical matrix proteins from filament proteins in wool. Through differential labelling of cysteine residues their relative accessibility in the wool fibre has been investigated. This has allowed the preliminary development of a map of the chemical functionality that is accessible within wool fibres under native conditions. Protein analyses of wool subjected to mechanical action, wet chemical permonosulphate/sulphite treatment and dry argon plasma treatment revealed that none of these detectably improved the accessibility of functional groups at the wool cortex. It is anticipated that this analytical method can be extended to improve the sensitivity and scope with which chemical functionality within native fibres can be mapped and lead to a better understanding of the potential limits/opportunities for fibre modification. © 2011 Elsevier B.V.
    Original languageEnglish
    Pages (from-to)323-330
    Number of pages7
    JournalInternational Journal of Biological Macromolecules
    Volume49
    Issue number3
    DOIs
    Publication statusPublished - 1 Oct 2011

    Keywords

    • Accessible chemical functionality of protein
    • Alpha-helical protein structure
    • Disulphide bond reduction

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