Sequence clustering confounds AlphaFold2.

ABSTRACT: Though typically associated with a single folded state, some globular proteins remodel their secondary and/or tertiary structures in response to cellular stimuli. AlphaFold2¹ (AF2) readily generates one dominant protein structure for these fold-switching (a.k.a. metamorphic) proteins², but it often fails to predict their alternative experimentally observed structures^3,4. Wayment-Steele, et al. steered AF2 to predict alternative structures of a few metamorphic proteins using a method they call AF-cluster⁵. However, their Paper lacks some essential controls needed to assess AF-cluster's reliability. We find that these controls show AF-cluster to be a poor predictor of metamorphic proteins. First, closer examination of the Paper's results reveals th

SUBMITTER: Schafer JW 

PROVIDER: S-EPMC10836070 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature