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Photo Marie Skepö

Marie Skepö

Professor

Photo Marie Skepö

The Effects of Chain Length on the Structural Properties of Intrinsically Disordered Proteins in Concentrated Solutions

Author

  • Eric Fagerberg
  • Linda K. Mansson
  • Samuel Lenton
  • Marie Skepo

Summary, in English

Intrinsically disordered proteins (IDP) are proteins that sample a heterogeneous ensemble of conformers in solution. An estimated 25-30% of all eukaryotic proteins belong to this class. In vivo, IDPs function under conditions that are highly crowded by other biological macromolecules. Previous research has highlighted that the presence of crowding agents can influence the conformational ensemble sampled by IDPs, resulting in either compaction or expansion. The effects of self-crowding of the disordered protein Histatin 5 has, in an earlier study, been found to have limited influence on the conformational ensemble. In this study, it is examined whether the short chain length of Histatin 5 can explain the limited effects of crowding observed, by introducing (Histatin 5)2, a tandem repeat of Histatin 5. By utilizing small-angle X-ray scattering, it is shown that the conformational ensemble is conserved at high protein concentrations, in resemblance with Histatin 5, although with a lowered protein concentration at which aggregation arises. Under dilute conditions, atomistic molecular dynamics and coarse-grained Monte Carlo simulations, as well as an established scaling law, predicted more extended conformations than indicated by experimental data, hence implying that (Histatin 5)2 does not behave as a self-avoiding random walk.

Department/s

  • Computational Chemistry
  • LINXS - Institute of advanced Neutron and X-ray Science
  • eSSENCE: The e-Science Collaboration

Publishing year

2021

Language

English

Pages

11843-11853

Publication/Series

Journal of Physical Chemistry B

Volume

124

Issue

52

Document type

Journal article

Publisher

The American Chemical Society (ACS)

Topic

  • Biophysics
  • Theoretical Chemistry (including Computational Chemistry)

Status

Published

ISBN/ISSN/Other

  • ISSN: 1520-6106