Obsessively checking whether my alphafold runs are done is far more rewarding than any other obsessive checking I've ever engaged in (grant/paper reviews, buying tickets, registering for classes, checking for a e-mail response).
@MCDuncanLab also curious if these are mutants, or complexes, or super big proteins? I’ve been so grateful that Uniprot has already AlphaFolded every protein in the Naegleria genome (and most model organisms) so I actually haven’t had to wait for anything I’ve needed yet!
@MCDuncanLab so cool! I am still just figuring out what can be done so I’m excited to see what you do with this
In this preprint, we identified a conserved or suspiciously structurally similar interface between a large highly conserved well-folded protein and its fast-evolving co-factors in yeast and humans. Some of the co-factors are large, but all of them consist primarily of disordered regions.
https://www.biorxiv.org/content/10.1101/2023.08.24.554671v2
We are now using alpha fold to predict protein-protein interactions amongst proteins that are linked to these ones via phenomics.
@askennard
Big proteins forming complexes.