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.

⌋International Clinical Research Center St Anne's University Hospital Brno Pekarska 53 656 91 Brno Czech Republic

†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

‡Loschmidt Laboratories Department of Experimental Biology and Research Centre for Toxic Compounds in the Environment RECETOX Faculty of Science Masaryk University Kamenice 5 A13 625 00 Brno Czech Republic

∥Department of Chemistry Faculty of Science Masaryk University Kamenice 5 A13 625 00 Brno Czech Republic

Citace poskytuje Crossref.org

Mechanism-Based Strategy for Optimizing HaloTag Protein Labeling

What Does Time-Dependent Fluorescence Shift (TDFS) in Biomembranes (and Proteins) Report on?

Fluorescent substrates for haloalkane dehalogenases: Novel probes for mechanistic studies and protein labeling

Solvatochromic fluorene-linked nucleoside and DNA as color-changing fluorescent probes for sensing interactions