Assessing the relation between protein phosphorylation, AlphaFold3 models, and conformational variability.

ABSTRACT: Proteins perform diverse functions critical to cellular processes. Transitions between functional states are often regulated by post-translational modifications (PTMs) such as phosphorylation, which dynamically influence protein structure, function, folding, and interactions. Dysregulation of PTMs can therefore contribute to diseases such as cancer and Alzheimer's. However, the structure-function relationship between proteins and their modifications remains poorly understood due to a lack of experimental structural data, the inherent diversity of PTMs, and the dynamic nature of proteins. Recent advances in deep learning, particularly AlphaFold, have transformed protein structure prediction with near-experimental accuracy. However, it remains unclear whether these models can effectively cap

SUBMITTER: Ramasamy P 

PROVIDER: S-EPMC12723721 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature