I have used AlphaFold a bit in my own work, and if I showed it 'unusual' proteins like rare mutants it usually generated garbage. Some evidence for this exists in the literature; see for example https://www.biorxiv.org/content/10.1101/2021.09.19.460937v1 or https://academic.oup.com/bioinformatics/article/38/7/1881/65... or
>AlphaFold recognizes a 3D structure of the examined amino acid sequence by a similarity of this sequence (or its parts) to related sequences with already known 3D structures
https://www.biorxiv.org/content/10.1101/2022.11.21.517308v1
I have used AlphaFold a bit in my own work, and if I showed it 'unusual' proteins like rare mutants it usually generated garbage. Some evidence for this exists in the literature; see for example https://www.biorxiv.org/content/10.1101/2021.09.19.460937v1 or https://academic.oup.com/bioinformatics/article/38/7/1881/65... or
>AlphaFold recognizes a 3D structure of the examined amino acid sequence by a similarity of this sequence (or its parts) to related sequences with already known 3D structures
https://www.biorxiv.org/content/10.1101/2022.11.21.517308v1