Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 50,135 bioRxiv papers from 233,681 authors.
Biological Structure and Function Emerge from Scaling Unsupervised Learning to 250 Million Protein Sequences
In the field of artificial intelligence, a combination of scale in data and model capacity enabled by unsupervised learning has led to major advances in representation learning and statistical generation. In biology, the anticipated growth of sequencing promises unprecedented data on natural sequence diversity. Learning the natural distribution of evolutionary protein sequence variation is a logical step toward predictive and generative modeling for biology. To this end we use unsupervised learning to train a deep contextual language model on 86 billion amino acids across 250 million sequences spanning evolutionary diversity. The resulting model maps raw sequences to representations of biological properties without labels or prior domain knowledge. The learned representation space organizes sequences at multiple levels of biological granularity from the biochemical to proteomic levels. Learning recovers information about protein structure: secondary structure and residue-residue contacts can be extracted by linear projections from learned representations. With small amounts of labeled data, the ability to identify tertiary contacts is further improved. Learning on full sequence diversity rather than individual protein families increases recoverable information about secondary structure. We show the networks generalize by adapting them to variant activity prediction from sequences only, with results that are comparable to a state-of-the-art variant predictor that uses evolutionary and structurally derived features.
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