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Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins
- Source :
- Journal of chemical theory and computation. 18(10)
- Publication Year :
- 2023
-
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.
Details
- ISSN :
- 15499626
- Volume :
- 18
- Issue :
- 10
- Database :
- OpenAIRE
- Journal :
- Journal of chemical theory and computation
- Accession number :
- edsair.doi.dedup.....7304c69c42b55837d49c1a72a85d1d41