Higher sequence coverage and improved confidence in the identification of cysteine-rich proteins from the wool cuticle using combined chemical and enzymatic digestion

Keratin-associated proteins are important constituents of the wool cuticle, comprised of the endo, exocuticle and a-layers, which contribute significantly to the fibre's molecular and mechanical characteristics

Henning Koehn; Stefan Clerens; Santanu Deb-Choudhury; James D. Morton; Jolon M. Dyer; Jeffrey E. Plowman

2009

Key concepts

Scholarcy highlights

  • Keratin-associated proteins are important constituents of the wool cuticle, comprised of the endo, exocuticle and a-layers, which contribute significantly to the fibre's molecular and mechanical characteristics
  • Little is known about the distribution of specific KAPs across these layers, and correct protein identification of individual KAPs is difficult due to extensive homology and identity among individual KAPs
  • Some of the peptides found to be unique to particular KAPs could only be found in either the exo- or endocuticle
  • We conclude that for the analysis of high sulphur proteomes, specific targeting of cysteine residues using chemical agents such as nitro-5-thiocyanobenzoic acid can provide critical information for unambiguous protein identification

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