You are here:
Publication details
Site-specific Analysis of Protein Hydration Based on Unnatural Amino Acid Fluorescence.
Authors | |
---|---|
Year of publication | 2015 |
Type | Article in Periodical |
Magazine / Source | Journal of the American Chemical Society |
MU Faculty or unit | |
Citation | |
Web | http://loschmidt.chemi.muni.cz/peg/wp-content/uploads/2015/04/jacs15.pdf |
Doi | http://dx.doi.org/10.1021/jacs.5b01681 |
Field | Biochemistry |
Keywords | dehalogenases;fluorescence spectroscopy;molecular dynamics simulations |
Description | 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. |
Related projects: |