Deep learning for intrinsically disordered proteins: From improved predictions to deciphering conformational ensembles.

Curr Opin Struct Biol

Department of Biochemistry, Eötvös Loránd University, Pázmány Péter stny 1/c, Budapest H-1117, Hungary. Electronic address:

Published: December 2024

Intrinsically disordered proteins (IDPs) lack a stable three-dimensional structure under physiological conditions, challenging traditional structure-based prediction methods. This review explores how modern deep learning approaches, which have revolutionized structure prediction for globular proteins, have impacted protein disorder predictions. We highlight the role of community-driven efforts in curating data and assessing state-of-the-art, which have been crucial in advancing the field. We also review state-of-the-art methods utilizing deep learning techniques, highlighting innovative approaches. We also address advancements in characterizing protein conformational ensembles directly from sequence data using novel machine learning methods.

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http://dx.doi.org/10.1016/j.sbi.2024.102950DOI Listing

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