For half a century, scientists struggled to predict how proteins fold. A puzzle at the heart of understanding life and curing disease. Then, five years ago, the #alphafold team cracked the code.
Since then, more than 3 million researchers across 190+ countries have used AlphaFold’s freely available database of 200 million+ protein structures, accelerating discoveries in everything from drug design to disease-resistant crops, bee conservation, and plastic-eating enzymes.
Learn more: https://deepmind.google/blog/alphafold-five-years-of-impact
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Further reading:
Here are just a few examples of how researchers worldwide are using AlphaFold (in order of appearance):
Chile, Germany: Engineering the catalytic activity of an Antarctic PET-degrading enzyme by loop exchange: https://onlinelibrary.wiley.com/doi/abs/10.1002/pro.4757
United Kingdom: AlphaFold-Multimer predicts cross-kingdom interactions at the plant-pathogen interface: https://www.nature.com/articles/s41467-023-41721-9
United States: Increasing thermostability of the key photorespiratory enzyme glycerate 3-kinase by structure-based recombination: https://onlinelibrary.wiley.com/doi/10.1111/pbi.14508
United States: The structure of apolipoprotein B100 from human low-density lipoprotein: https://www.nature.com/articles/s41586-024-08467-w
Norway, Portugal, USA, UK: Cryo-EM structure of native honey bee vitellogenin: https://www.nature.com/articles/s41467-025-58575-y
Spain: Identification of novel compounds against Trypanosoma cruzi using AlphaFold structures: https://linkinghub.elsevier.com/retrieve/pii/S2001037025001655
France: Structural basis for hepatitis E virus neutralization by potent human antibodies: https://www.science.org/doi/full/10.1126/sciadv.adu8811
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