Advances in Prediction of Posttranslational Modification Sites Known to Localize in Protein Supersecondary Structures
Document Type
Article
Publication Date
2025
Department
Department of Computer Science
Abstract
Posttranslational modifications (PTMs) play a crucial role in modulating the structure, function, localization, and interactions of proteins, with many PTMs being localized within supersecondary structures, such as helical pairs. These modifications can significantly influence the conformation and stability of these structures. For instance, phosphorylation introduces negative charges that alter electrostatic interactions, while acetylation or methylation of lysine residues affects the stability and interactions of alpha helices or beta strands. Given the pivotal role of supersecondary structures in the overall protein architecture, their modulation by PTMs is essential for protein functionality. This chapter explores the latest advancements in predicting sites for the five PTMs (phosphorylation, acetylation, glycosylation, methylation, and ubiquitination) known to be localized within supersecondary structures. The chapter highlights the recent advances in the prediction of these PTM sites, including the use of global contextualized embeddings from protein language models, integration of structural information, utilization of reliable positive and negative sites, and application of contrastive learning. These methodologies and emerging trends offer a roadmap for novel innovations in addressing PTM prediction challenges, particularly those linked to supersecondary structures.
Publication Title
Methods in molecular biology (Clifton, N.J.)
Recommended Citation
Pratyush, P.,
&
KC, D.
(2025).
Advances in Prediction of Posttranslational Modification Sites Known to Localize in Protein Supersecondary Structures.
Methods in molecular biology (Clifton, N.J.),
2870, 117-151.
http://doi.org/10.1007/978-1-0716-4213-9_8
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p2/1328
