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Many immune receptors function in pairs called dimers, but to date, PD-1 has been thought to function alone, not in the dimer form.

Further analysis using X-ray crystallography and thermodynamic simulations revealed that tetramer formation is driven by hydrophobic interactions occurring between two 3D-DS dimers.

After one particularly bad morning, an urgent care visit revealed that she had high blood levels of “D dimer,” a protein fragment that indicates the presence of clots.

This suggested that individual toroids could act as secondary sites from which another ring could grow, thereby forming the catenated dimers.

I decided to use an icosahedral sphere to create a regular distribution of the M protein dimers to hint at this hypothesis.