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bioRxiv · 10.1101/2022.02.11.480128

Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins

Dey, S.·MacAinsh, M.·Zhou, H.-X.
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Abstract

For intrinsically disordered proteins (IDPs), a pressing question is how sequence codes for function. Dynamics serves as a crucial link, reminiscent of the role of structure in sequence-function relations of structured proteins. To define general rules governing sequence-dependent backbone dynamics, we carried out long molecular dynamics simulations of eight IDPs. Blocks of residues exhibiting large amplitudes in slow dynamics are rigidified by local inter-residue interactions or secondary structures. A long region or an entire IDP can be slowed down by long-range contacts or secondary- structure packing. On the other hand, glycines promote fast dynamics and either demarcate rigid blocks or facilitate multiple modes of local and long-range inter-residue interactions. The sequence-dependent backbone dynamics endows IDPs with versatile response to binding partners, with some blocks recalcitrant while others readily adapting to intermolecular interactions.

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Dey, S., MacAinsh, M., Zhou, H.-X.. 2022-02-12. Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins. https://doi.org/10.1101/2022.02.11.480128

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