Despite recent progress 10, 11, 12, 13, 14, existing methods fall far short of atomic accuracy, especially when no homologous structure is available. Predicting the three-dimensional structure that a protein will adopt based solely on its amino acid sequence-the structure prediction component of the ‘protein folding problem’ 8-has been an important open research problem for more than 50 years 9. Accurate computational approaches are needed to address this gap and to enable large-scale structural bioinformatics.
Structural coverage is bottlenecked by the months to years of painstaking effort required to determine a single protein structure. Through an enormous experimental effort 1, 2, 3, 4, the structures of around 100,000 unique proteins have been determined 5, but this represents a small fraction of the billions of known protein sequences 6, 7. Proteins are essential to life, and understanding their structure can facilitate a mechanistic understanding of their function.
Nature volume 596, pages 583–589 ( 2021) Cite this article Highly accurate protein structure prediction with AlphaFold
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