Check out DeepMind's AlphaFold - and marvel at the complex 3D structure of proteins - at https://alphafold.ebi.ac.uk/
A simple mis-folding in a certain brain protein causes a disease for which we have no cure.
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To learn more about this topic, start your googling with these keywords:
- Prion: an abnormal pathogenic agent that is transmissible and able to induce abnormal folding of specific normal cellular proteins called prion proteins that are found most abundantly in the brain.
- Spongiform encephalopathies: a group of rare degenerative brain disorders caused by prions and characterized by tiny holes that give the brain a “spongy” appearance.
- Amyloid: an abnormal aggregate of protein.
- Creutzfeldt-Jakob disease: also known as subacute spongiform encephalopathy or neurocognitive disorder due to prion disease, is an invariably fatal degenerative brain disorder. Early symptoms include memory problems, behavioral changes, poor coordination, and visual disturbances. Later symptoms include dementia, involuntary movements, blindness, weakness, and coma. About 70% of people die within a year of diagnosis.
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REFERENCES
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Dabin LC, Guntoro F, Campbell T, Bélicard T, Smith AR, Smith RG, Raybould R, Schott JM, Lunnon K, Sarkies P, Collinge J, Mead S, Viré E (2020). Altered DNA methylation profiles in blood from patients with sporadic Creutzfeldt-Jakob disease. Acta Neuropathology 140(6):863-879. https://doi.org/10.1007/s00401-020-02224-9
Miller G. (2009) Neurodegeneration. Acting like a prion isn't always bad. Science 326 (5958):1338. https://doi.org/10.1126/science.326.5958.1338
Quartararo, AJ. (2020) Synthesis of Proteins by Automated Flow Chemistry. Science 368 (6494): 980– 987, https://doi.org/10.1126/science.abb2491
Sabate R. (2014) When amyloids become prions. Prion 8 (3):233-9. https://doi.org/10.4161/19336896.2014.968464
Scheckel, C., Aguzzi, A. (2018) Prions, prionoids and protein misfolding disorders. Nature Reviews Genetics 19, 405–418. https://doi.org/10.1038/s41576-018-0011-4
Vastag, B. (2009) The beneficial side of prions. Nature https://doi.org/10.1038/news.2009.23