ArticleThe European physical journal. E, Soft matter2013
The effect of complex solvents on the structure and dynamics of protein solutions: The case of Lysozyme in trehalose/water mixtures.
Article in The European physical journal. E, Soft matter, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- Not only an inhibitor: Trehalose enhances the catalytic action exerted on oxaloacetate by rabbit lactate dehydrogenase.Protein science : a publication of the Protein Society · 2025Article
- Mechanistic differences in the effects of sucrose and sucralose on the phase stability of lysozyme solutions.Journal of molecular liquids · 2021Article
- Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.Computational and structural biotechnology journal · 2017Review
- The gene expression level of IFN-γR1 and IFN-γR2 in a murine model treated with Toxoplasma gondii and its products.Gastroenterology and hepatology from bed to bench · 2016Article
- A molecular simulation study of the protection of insulin bioactive structure by trehalose.Journal of molecular modeling · 2014Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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Abstract
We present a Molecular Dynamics simulation study of the effect of trehalose concentration on the structure and dynamics of individual proteins immersed in trehalose/water mixtures. Hen egg-white Lysozyme is used in this study and trehalose concentrations of 0%, 10%, 20%, 30% and 100% by weight are explored. Surprisingly, we have found that changes in trehalose concentration do not change the global structural characteristics of the protein as measured by standard quantities like the mean square deviation, radius of gyration, solvent accessible surface area, inertia tensor and asphericity. Only in the limit of pure trehalose these metrics change significantly. Specifically, we found that the protein is compressed by 2% when immersed in pure trehalose. At the amino acid level there is noticeable rearrangement of the surface residues due to the change in polarity of the surrounding environment with the addition of trehalose. From a dynamic perspective, our computation of the Incoherent Intermediate Scattering Function shows that the protein slows down with increasing trehalose concentration; however, this slowdown is not monotonic. Finally, we also report in-depth results for the hydration layer around the protein including its structure, hydrogen-bonding characteristics and dynamic behavior at different length scales.
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