ArticleComputational and structural biotechnology journal2025
Comprehensive assessment of AlphaFold's predictions of secondary structure and solvent accessibility at the amino acid-level in eukaryotic, bacterial and archaeal proteins.
Article in Computational and structural biotechnology journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- In silico conformational dynamics of the α-actinin-2 actin-binding domain upon phosphorylation.Biophysical journal · 2026Article
- AlphaFold in protein structure and function prediction.Computational and structural biotechnology journal · 2025Article
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3 authors.
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Abstract
Numerous sequence-based predictors of the amino acid (AA)-level solvent accessibility (SA) and secondary structure (SS) of proteins have been developed. We empirically investigated whether these two key characteristics of AA-level structure can be accurately predicted from putative structures generated by the popular AlphaFold2. We compared AlphaFold2's results against several representative SS and SA predictors on a large test dataset that covers five distinct taxonomic groups (animals, plants, fungi, bacteria, and archaea). We used a broad collection of metrics that evaluate predictions of the numeric and binary (buried vs. solvent exposed) SA and the 3-state SS at both AA- and SS-region levels. We found that AlphaFold2 generated very accurate results, with high average Q
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