Szczegóły publikacji
Opis bibliograficzny
EsmTemp - transfer learning approach for predicting protein thermostability / Adam Sułek, Jakub Jończyk, Patryk Orzechowski, Ahmed Abdeen Hamed, Marek WODZIŃSKI // W: Computational Science – ICCS 2024 : 24th International Conference : Malaga, Spain, July 2–4, 2024 : proceedings, Pt. 3 / eds. Leonardo Franco, [et al.]. — Cham : Springer, cop. 2024. — (Lecture Notes in Computer Science ; ISSN 0302-9743 ; 14834). — ISBN: 978-3-031-63758-2; e-ISBN: 978-3-031-63759-9. — S. 187–194. — Bibliogr., Abstr. — Publikacja dostępna online od: 2024-06-29. — M. Wodziński - dod. afiliacja: University of Applied Sciences Western Switzerland, Sierre, Switzerland
Autorzy (5)
- Sułek Adam
- Jończyk Jakub
- Orzechowski Patryk
- Hamed Ahmed Abdeen
- AGHWodziński Marek
Dane bibliometryczne
| ID BaDAP | 154327 |
|---|---|
| Data dodania do BaDAP | 2024-07-12 |
| DOI | 10.1007/978-3-031-63759-9_23 |
| Rok publikacji | 2024 |
| Typ publikacji | materiały konferencyjne (aut.) |
| Otwarty dostęp |  |
| Wydawca | Springer |
| Konferencja | International Conference on Computational Science 2024 |
| Czasopismo/seria | Lecture Notes in Computer Science |
Abstract
Protein thermostability is one of the most important features of bio-engineered proteins with significant scientific and industrial applications. Unfortunately, obtaining thermostable proteins is both expensive and complex. Recent advances in Protein Language Models (pLM) offer promising framework for sequence-to-sequence problems, especially in the realm of protein thermostability prediction. In this work, we present EsmTemp, a transfer learning model based on the ESM-2 pLM architecture. EsmTemp undergoes training on a meticulously curated dataset comprising 24,000 protein sequences with known melting temperatures. A rigorous evaluation, conducted through a 10-fold cross-validation, yields a coefficient of determination (R2) of 0.70 and a mean absolute error of 4.3°C. These outcomes highlight how pLM has the potential to advance our understanding of protein thermostability and facilitate the rational design of enzymes for various applications.
