Macromolecular crowding and the importance of proper hydration for the structure and dynamics of protein solutions

Phys Chem Chem Phys. 2018 Jul 25;20(29):19581-19594. doi: 10.1039/c8cp02360c.

Abstract

Recent experiments by Weingärtner et al. have given a first hint that dielectric spectroscopy is able to yield a quantitative measure of inter-protein mutual orientation. Therefore, in this computational study, we investigate crowded multi-protein solutions with a special focus on this mutual orientation and its context with dielectric spectroscopy. To the end, existing standard force fields had to be improved by re-scaling the dispersion interaction between protein and water. We find that proper hydration has a strong influence on inter-protein correlations as an enhancement of protein hydration by 10% has a great impact on orientational intermolecular structure. Altogether, the crowding behaviour is improved considerably.

MeSH terms

  • Macromolecular Substances / chemistry
  • Molecular Dynamics Simulation*
  • Protein Conformation
  • Solutions
  • Ubiquitin / chemistry*
  • Water / chemistry

Substances

  • Macromolecular Substances
  • Solutions
  • Ubiquitin
  • Water