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The effects of chain length on the structural properties of intrinsically disordered proteins in concentrated solutions

DOI: 10.1021/acs.jpcb.0c09635 DOI Help

Authors: Eric Fagerberg (Lund University) , Linda K. Månsson (Lund University) , Samuel Lenton (Lund University; LINXS - Lund Institute of Advanced Neutron and X-ray Science) , Marie Skepö (Lund University; LINXS - Lund Institute of Advanced Neutron and X-ray Science)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Journal Of Physical Chemistry B , VOL 124 , PAGES 11843 - 11853

State: Published (Approved)
Published: December 2020
Diamond Proposal Number(s): 23750

Open Access Open Access

Abstract: 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.

Journal Keywords: Salts; Monte Carlo simulations; Algorithms; X-ray scattering; Nucleic acid structure

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: B21-High Throughput SAXS

Added On: 03/01/2021 10:30

Documents:
acs.jpcb.0c09635.pdf

Discipline Tags:

Physical Chemistry Chemistry Organic Chemistry

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)