Highly accurate protein structure prediction with AlphaFold (with 33 co-authors)

Demis Hassabis · 15 Jul 2021 · doi.org ↗

4 korrents from this paper

In plain words

A computer program regularly predicts a protein's three-dimensional shape from its amino acid sequence alone at accuracy matching lab experiments, even with no similar structure known. It opens large-scale study of how proteins work since experiments have solved only around 100,000 while billions of sequences are known and each takes months to years. It reports results from a redesigned neural network incorporating physical and biological knowledge that greatly outperformed other methods in a blind test.

Our summary of the paper, not the authors' words — written to be readable without the field's vocabulary, from the stored copy of the paper and nothing else. Drafted with xai:grok-4.5 and checked by a person. The authors' own sentences are the quotes below.

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Our reading
Accurate computational approaches are needed to close the protein structural coverage gap and enable large-scale structural bioinformatics.

Their wordsAccurate computational approaches are needed to address this gap and to enable large-scale structural bioinformatics.
Our reading
Existing protein structure prediction methods fall far short of atomic accuracy when no homologous structure is available.

Their wordsDespite recent progress10-14, existing methods fall far short of atomic accuracy, especially when no homologous structure is available.
Our reading
A computational method can regularly predict protein structures with atomic accuracy even when no similar structure is known.

Their wordsHere we provide the first computational method that can regularly predict protein structures with atomic accuracy even in cases in which no similar structure is known.
Our reading
Contemporary physical and evolutionary structure-prediction approaches fall far short of experimental accuracy without a close experimental homologue, limiting biological utility.

Their wordsDespite these advances, contemporary physical and evolutionary-history-based approaches produce predictions that are far short of experimental accuracy in the majority of cases in which a close homologue has not been solved experimentally and this has limited their utility for many biological applications.