Design of intrinsically disordered protein variants with diverse structural properties

Supporting data and code for:

Pesce, F., Bremer, A., Tesei, G., Hopkins, J. B., Grace, C. R., Mittag, T., & Lindorff-Larsen, K. (2023). Design of intrinsically disordered protein variants with diverse structural properties. bioRxiv.

Molecular dynamics simulations are available on ERDA.

Data also available on ZENODO.

List of content:

• CODE: Python code to reproduce simulations (single- and multi-chain) and run the design algorithm (using Rg or contact maps as structural targets).
• EVOLUTION_DATA: Data produced by running the design algorithm.
• NMR: Raw PFG-NMR measurements of A1-LCD and V1 at 34°C.
• SAXS: Solvent subtracted and averaged SEC-SAXS measurements of A1-LCD and V2–V5.
• 120centroids_data.pkl: Sequences, Rg and sequence features of 120 representative A1-LCD swap variants generated by designing more compact variants.
• Figures.ipynb: Jupyter notebook to reproduce the figures in the main text of the paper.
• IDPDesigner.ipynb: Google Colab notebook to design IDP sequences with a specific scaling exponent.
• V1-5_WT_csat.xlsx: Measured saturation concentration values for A1-LCD and V1–V5.
• exp_sequences.fasta: Sequences of A1-LCD and V1–V5 experimentally characterized.
• no_expression_sequences.fasta: Sequences of swap variants of A1-LCD that did not express in E. coli.