Site-specific analysis of protein hydration based on unnatural amino acid fluorescence
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
25815779
DOI
10.1021/jacs.5b01681
Knihovny.cz E-resources
- MeSH
- Amino Acids chemistry MeSH
- Fluorescence * MeSH
- Molecular Structure MeSH
- Proteins chemistry MeSH
- Molecular Dynamics Simulation MeSH
- Water analysis chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Amino Acids MeSH
- Proteins MeSH
- Water MeSH
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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