Co-translational protein folding is shaped by the vectorial nature of translation, in which amino acid residues emerge sequentially from the ribosome. As a result, residues whose native interaction partners are encoded further downstream in the sequence cannot immediately form their native contacts and remain transiently unsatisfied until those partners are synthesized. Residues that persist in an unsatisfied state for extended periods are particularly susceptible to misfolding and often engage co-translational factors such as molecular chaperones.

The FoldDelay web server is a web-based tool that estimates the time required for native residue-residue contacts to form during translation. The server provides a suite of linked interactive visualizations that allows users to explore native contact formation dynamics and detect transiently unsatisfied regions in their structural context.

A standalone version of FoldDelay is also available for local use and is recommended for large-scale screens. The script can be accessed at https://github.com/ramondur/Native-Fold-Delay.

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References

When using this website, please cite the following:

• Duran-Romana, R., et al., Native Fold Delay and its implications for co-translational chaperone binding and protein aggregation. Nat Commun, 2025. 16(1): p. 1673. https://doi.org/10.1038/s41467-025-57033-z