Intrinsic protein disorder and conditional folding in AlphaFoldDB

By Damiano Piovesan, Alexander Miguel Monzon, Silvio C. E. Tosatto. 2022

134 citations recorded by the source corpus.

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.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Damiano Piovesan
2. Silvio C. E. Tosatto
3. Liam J. McGuffin
4. Pascal Benkert

In Molecular Biology

1. Damiano Piovesan
2. Silvio C. E. Tosatto
3. Zsuzsanna Dosztányi
4. Liam J. McGuffin
5. Pascal Benkert

In Spectroscopy

1. Silvio C. E. Tosatto

Citations in the corpus

• Critical assessment of protein intrinsic disorder prediction (CAID) ‐ Results of round 2 (2023, methodology): “The specific formula used for AlphaFold-disorder predictions is outlined in reference 9.”