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
”
![Image of study](/images/research/0d450632-470a-4dfb-87d2-f64556cf754e/medium/36995.jpg)
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.