Molecular Modeling and Structural Characterization of a High Glycine–Tyrosine Hair Keratin Associated Protein

    Rakesh S. Singh, Jeremy C. Palmer, Paul D. A. Pudney, Prem K. C. Paul, Christian Johannessen, Pablo G. Debenedetti, Janhavi S. Raut, Ken Lee, Massimo G. Noro, David Tiemessen
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    TLDR The 3D structure of a key hair protein was modeled, revealing specific helical structures and stabilization features.
    The study focused on characterizing the high glycine-tyrosine (HGT) protein KAP8.1, a key component of keratin associated proteins (KAPs) in human hair, through computational modeling and experimental methods. The researchers modeled the 3D structure of the 63-residue KAP8.1 protein, revealing it to have four poly-proline II helical structures stabilized by two cysteine disulphide bridges. Both computer simulations and spectroscopic studies (Raman, IR, and vibrational circular dichroism) confirmed the presence of β-sheet and PPII structures. This work provided a foundational model for further studies on the glassy state physics of hair, aiming to understand how hair properties can be influenced by environmental factors and additives.
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