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Plowman JE, Miller RE, Thomas A, et al. A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres. Proteins. 2021;89(6):708-720doi: 10.1002/prot.26053.
Plowman, J. E., Miller, R. E., Thomas, A., Grosvenor, A. J., Harland, D. P., & Deb-Choudhury, S. (2021). A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres. Proteins, 89(6), 708-720. https://doi.org/10.1002/prot.26053
Plowman, Jeffrey E, et al. "A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres." Proteins vol. 89,6 (2021): 708-720. doi: https://doi.org/10.1002/prot.26053
Plowman JE, Miller RE, Thomas A, Grosvenor AJ, Harland DP, Deb-Choudhury S. A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres. Proteins. 2021 Jun;89(6):708-720. doi: 10.1002/prot.26053. Epub 2021 Feb 22. PMID: 33550642.
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Proteins. 2021 Jun;89(6):708-720. doi: 10.1002/prot.26053. Epub 2021 Feb 22.

A detailed mapping of the readily accessible disulphide bonds in the cortex of wool fibres.

Proteins

Jeffrey E Plowman, Rachel E Miller, Ancy Thomas, Anita J Grosvenor, Duane P Harland, Santanu Deb-Choudhury

Affiliations

  1. Proteins and Metabolites, AgResearch, Christchurch, New Zealand.

PMID: 33550642 DOI: 10.1002/prot.26053

Abstract

Trichocyte keratin intermediate filament proteins (keratins) and keratin associated proteins (KAPs) differ from their epithelial equivalents by having significantly more cysteine residues. Interactions between these cysteine residues within a mammalian fiber, and the putative regular organization of interactions are likely important for defining fiber mechanical properties, and thus biological functionality of hairs. Here we extend a previous study of cysteine accessibility under different levels of exposure to reducing compounds to detect a greater resolution of statistically non-random interactions between individual residues from keratins and KAPs. We found that most of the cysteines with this non-random accessibility in the KAPs were close to either the N- or C- terminal domains of these proteins. The most accessible non-random cysteines in keratins were present in the head or tail domains, indicating the likely function of cysteine residues in these regions is in readily forming intermolecular bonds with KAPs. Some of the less accessible non-random cysteines in keratins were discovered either close to or within the rod region in positions previously identified in human epithelial keratins as involved in crosslinking between the heterodimers of the tetramer. Our present study therefore provides a deeper understanding of the accessibility of disulfides in both keratins and KAPs and thus proves that there is some specificity to the disulfide bond interactions leading to these inter- and intra-molecular bonds stabilizing the fiber structure. Furthermore, these suggest potential sites of interaction between keratins and KAPs as well as keratin-keratin interactions in the trichocyte intermediate filament.

© 2021 Wiley Periodicals LLC.

Keywords: Trichocyte keratins; accessibility mapping; keratin associated proteins; mass spectrometry; protein chemistry

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