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IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins (IDP) Using Large Language Models

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arxiv 2403.19762 v2 pith:TASLZQDV submitted 2024-03-28 q-bio.BM

classification q-bio.BM
keywords proteinsidpsfunctionspropertiesbiologicalclassdisorderedexperiments
verification ladder T0 review T1 audit T2 compute T3 formal
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Intrinsically Disordered Proteins (IDPs) constitute a large and structure-less class of proteins with significant functions. The existence of IDPs challenges the conventional notion that the biological functions of proteins rely on their three-dimensional structures. Despite lacking well-defined spatial arrangements, they exhibit diverse biological functions, influencing cellular processes and shedding light on the disease mechanisms. However, it is expensive to run experiments or simulations to characterize this class of proteins. Consequently, we designed an ML model that relies solely on amino acid sequences. In this study, we introduce IDP-Bert model, a deep-learning architecture leveraging Transformers and Protein Language Models (PLMs) to map sequences directly to IDPs properties. Our experiments demonstrate accurate predictions of IDPs properties, including Radius of Gyration, end-to-end Decorrelation Time, and Heat Capacity.

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Cited by 1 Pith paper

Reviewed papers in the Pith corpus that reference this work. Sorted by Pith novelty score. Full citation record

  1. Into the Unknown: From Structure to Disorder in Protein Function Prediction

    q-bio.BM 2025-06 conditional novelty 4.0 of 10

    A review with a small benchmark concluding that general protein function predictors underperform on disordered proteins, while IDR-specific FAIDR produces more specific GO annotations.

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