We started our simulation strategy by modeling the protein segment which will provide the anchoring points to the outermost 18-MEA molecules (see Figure ). In a previous study , the antifreeze protein from snow fleas was employed to this end. Despite having a less than 33 % homology with the full length KAP5-1 sequence, the snow flea antifreeze protein also contains glycine-rich repeats in its sequence, with a similar overall glycine content (33% composition) compared to KAP5-1. KAP8-1, a related KAP protein, has been successfully been modeled using the snow flea antifreeze protein structure template, and validated through a combination of Raman, infrared, and vibrational circular dichroism studies (Singh et al., 2017). Moreover, (i) there are no experimentally determined KAP structures, with all AlphaFold predicted structures for the KAP family primarily disordered and containing very low overall per-residue confidence scores ; (ii) secondary structure predictions of hair KAP sequences identified β sheets, β turns, disordered coil regions but no α helices; (iii) glycine-rich repeats are predicted to form β turn stacks in KAP5-1 .