A sequence-based method for predicting extant fold switchers that undergo α-helix ↔ β-strand transitions.

ABSTRACT: Extant fold-switching proteins remodel their secondary structures and change their functions in response to cellular stimuli, regulating biological processes and affecting human health. Despite their biological importance, these proteins remain understudied. Predictive methods are needed to expedite the process of discovering and characterizing more of these shapeshifting proteins. Most previous approaches require a solved structure or all-atom simulations, greatly constraining their use. Here, we propose a high-throughput sequence-based method for predicting extant fold switchers that transition from α-helix in one conformation to β-strand in the other. This method leverages two previous observations: (a) α-helix ↔ β-strand prediction discrepancies from JPred4 are a robust predictor of fo

SUBMITTER: Mishra S 

PROVIDER: S-EPMC8545793 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature