Theoretical models: Difference between revisions
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===2024 CASP 16=== | ===2024 CASP 16=== | ||
AlphaFold 2 & 3 have largely solved prediction of protein monomers and domains, "with barely any space for further improvements at the backbone level except for very specific details, irregular secondary structures, and mutational effects that remain challenging to predict."<ref>PMID: 41088961</ref> | Overall, on all fronts, AF3's modeling capabilities are at or close to the state of the art.<ref name="abriata" /> Prediction of protein oligomer complex assemblies "remains an unsolved challenge."<ref>PMID: 41170922</ref> | ||
AlphaFold 2 & 3 have largely solved prediction of protein monomers and domains, "with barely any space for further improvements at the backbone level except for very specific details, irregular secondary structures, and mutational effects that remain challenging to predict."<ref name="abriata">PMID: 41088961</ref> For prediction of protein oligomer assemblies, AlphaFold-based methods "show progress, though complex topologies and in particular antibody-antigen interactions are still difficult. Notably, a priori knowledge of stoichiometry significantly aids assembly prediction. Protein-'''ligand''' co-folding with AF3 demonstrated strong potential for pose prediction, outperforming many participants and some dedicated docking tools in baseline tests, but several caveats hold as discussed. Ligand '''affinity''' prediction is totally unreliable. Nucleic acid structure prediction lags considerably ...."<ref name="abriata" /> | |||
===2022: CASP 15=== | ===2022: CASP 15=== | ||
