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Updated: Apr 15, 2026
Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
Site-specific analysis of protein hydration based on unnatural amino acid fluorescence
Mariana Amaro1, Jan Brezovský2,3, Silvia Kováčová4,3
1†J. Heyrovsky Institute of Physical Chemistry of the ASCR, v. v. i., Academy of Sciences of the Czech Republic, Dolejskova 3, 182 23 Prague 8, Czech Republic.
Abstract:
Hydration of proteins profoundly affects their functions. We describe a simple and general method for site-specific analysis of protein hydration based on the in vivo incorporation of fluorescent unnatural amino acids and their analysis by steady-state fluorescence spectroscopy. Using this method, we investigate the hydration of functionally important regions of dehalogenases. The experimental results are compared to findings from molecular dynamics simulations.
