Exploring hydrophilic sequence space to search for uncharted foldable proteins by AlphaFold2.

ABSTRACT: Proteins typically fold into unique three-dimensional structures largely driven by interactions between hydrophobic amino acids. This understanding has helped improve our knowledge of protein folding. However, recent research has shown an exception to this idea, demonstrating that specific threonine-rich peptides have a strong tendency to form β-hairpin structures, even in the highly hydrophilic amino acid sequences. This finding suggests that the hydrophilic amino acid sequence space still leaves room for exploring foldable amino acid sequences. In this study, we conducted a systematic exploration of the repetitive amino acid sequence space by AlphaFold2 (AF2), with a focus on sequences composed exclusively of hydrophilic residues, to investigate their potential for adopting unique struct

SUBMITTER: Tomita N 

PROVIDER: S-EPMC11936462 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature