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

Intrinsically disordered Proteins (IDPs) constitute a large and structureless 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 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 the IDP-Bert model, a deep-learning architecture leveraging Transformers and Protein Language Models to map sequences directly to IDP properties. Our experiments demonstrate accurate predictions of IDP properties, including Radius of Gyration, end-to-end Decorrelation Time, and Heat Capacity.

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Publication Details

Journal
The Journal of Physical Chemistry B
Published
2024-11-25
DOI
https://doi.org/10.1021/acs.jpcb.4c02507
Citations
8
Primary Topic
Protein Structure and Dynamics
Type
article
Field-Weighted Citation Impact
1.87

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article

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

Amir Barati Farimani, Chakradhar Guntuboina, Parisa Mollaei, Danush Sadasivam
8 citations
The Journal of Physical Chemistry B
Protein Structure and Dynamics
1.87
article

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

Amir Barati Farimani, Chakradhar Guntuboina, Parisa Mollaei, Danush Sadasivam
article en
8 citations

Abstract

Intrinsically disordered Proteins (IDPs) constitute a large and structureless 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 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 the IDP-Bert model, a deep-learning architecture leveraging Transformers and Protein Language Models to map sequences directly to IDP properties. Our experiments demonstrate accurate predictions of IDP properties, including Radius of Gyration, end-to-end Decorrelation Time, and Heat Capacity.

The Journal of Physical Chemistry BVol. 128(49)
Carnegie Mellon University (US)
Carnegie Mellon University
Openalex Percentile: Top 14%
Protein Structure and Dynamics
1.87
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IDP-Bert: Predicting Properties of Intrinsically Disordered Proteins Using Large Language Models — Amir Barati Farimani, Chakradhar Guntuboina, et al. · The Journal of Physical Chemistry B (2024) | TGRS Research Map | TGRS