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Intrinsic protein disorder and conditional folding in AlphaFoldDB.


ABSTRACT: Intrinsically disordered regions (IDRs) defying the traditional protein structure-function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR prediction. Here, we establish three baselines for IDR prediction from AlphaFoldDB models based on the recent CAID dataset. Surprisingly, AlphaFoldDB is highly competitive for predicting both IDRs and conditionally folded binding regions, demonstrating the plasticity of the disorder to structure continuum.

SUBMITTER: Piovesan D 

PROVIDER: S-EPMC9601767 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature

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Intrinsic protein disorder and conditional folding in AlphaFoldDB.

Piovesan Damiano D   Monzon Alexander Miguel AM   Tosatto Silvio C E SCE  

Protein science : a publication of the Protein Society 20221101 11


Intrinsically disordered regions (IDRs) defying the traditional protein structure-function paradigm have been difficult to analyze. The availability of accurate structure predictions on a large scale in AlphaFoldDB offers a fresh perspective on IDR prediction. Here, we establish three baselines for IDR prediction from AlphaFoldDB models based on the recent CAID dataset. Surprisingly, AlphaFoldDB is highly competitive for predicting both IDRs and conditionally folded binding regions, demonstratin  ...[more]

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