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

    January 2017 in “ Physical chemistry chemical physics/PCCP. Physical chemistry chemical physics ”
    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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