Macromolecular crowding and the importance of proper hydration for the structure and dynamics of protein solutions
| Autor: | Philipp Honegger, Othmar Steinhauser, Michael Schmollngruber |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Materials science
010304 chemical physics Macromolecular Substances Protein Conformation Ubiquitin Intermolecular force Water General Physics and Astronomy Context (language use) Molecular Dynamics Simulation 010402 general chemistry 01 natural sciences Crowding 0104 chemical sciences Dielectric spectroscopy Solutions Molecular dynamics Protein structure Chemical physics Yield (chemistry) 0103 physical sciences Physical and Theoretical Chemistry Macromolecular crowding |
| Zdroj: | Physical Chemistry Chemical Physics. 20:19581-19594 |
| ISSN: | 1463-9084 1463-9076 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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