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. |
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