AlphaFold's highly accurate protein structure prediction
Supplementary videos of the paper "Highly accurate protein structure prediction with AlphaFold," authored by John Jumper, Richard Evans, …, Demis Hassabis, and published in Nature (15 Jul 2021), doi: https://doi.org/10.1038/s41586-021-03....
"Supplementary Video 1: Video of the intermediate structure trajectory of the CASP14 target T1024 (LmrP) A two-domain target (408 residues). Both domains are folded early, while their packing is adjusted for a longer time."
"Supplementary Video 2: Video of the intermediate structure trajectory of the CASP14 target T1044 (RNA polymerase of crAss-like phage).A large protein (2180 residues), with multiple domains. Some domains are folded quickly, while others take a considerable amount of time to fold."
"Supplementary Video 3: Video of the intermediate structure trajectory of the CASP14 target T1064 (Orf8).A very difficult single-domain target (106 residues) that takes the entire depth of the network to fold."
"Supplementary Video 4: Video of the intermediate structure trajectory of the CASP14 target T1091.A multi-domain target (863 residues). Individual domains’ structure is determined early, while the domain packing evolves throughout the network. The network is exploring unphysical configurations throughout the process, resulting in long ‘strings’ in the visualization."