The application of Kirkwood-Buff theory to study hydration properties of α-amino acids

Z. Štefanič; B. Hribar-Lee

doi:10.5488/CMP.29.13801

Authors

Z. Štefanič Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia https://orcid.org/0009-0008-3837-3941
B. Hribar-Lee Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, Slovenia https://orcid.org/0000-0002-9029-588X

DOI:

https://doi.org/10.5488/CMP.29.13801

Keywords:

amino acid, apparent molar volume, standard molar volume, hydration number, integral equation, Kirkwood-Buff theory

Abstract

Protein conformational stability and function depend on non-covalent interactions that are strongly influenced by the surrounding environment. To explore protein properties, amino acids are often utilized as model systems. In this study, we determined the densities of seven α-amino acids in aqueous solutions between 278.15 K and 308.15 K and calculated the apparent molar volumes. Linear extrapolation yielded standard molar volumes, which were analyzed to characterize amino-acid hydration. The contributions of side chains to the standard molar volume were determined relative to glycine. The standard molar volume increased with temperature, indicating reduced electrostriction of water around the amino acids, consistent with lower hydration numbers at higher temperatures. We employed the Ornstein-Zernike integral equation with hypernetted-chain closure and a coarse-grained Lennard-Jones bead model to calculate pair correlation functions and Kirkwood-Buff integrals, from which standard molar volumes were obtain. The model reproduced the experimental standard molar volumes very well.

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