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- W2078336233 abstract "Scientists have made tremendous efforts to gain understanding of the water molecules in proteins via indirect measurements such as molecular dynamic simulation and/or probing the polarity of the local environment. Here we present a tryptophan analogue that exhibits remarkable water catalysed proton-transfer properties. The resulting multiple emissions provide unique fingerprints that can be exploited for direct sensing of a site-specific water environment in a protein without disrupting its native structure. Replacing tryptophan with the newly developed tryptophan analogue we sense different water environments surrounding the five tryptophans in human thromboxane A₂ synthase. This development may lead to future research to probe how water molecules affect the folding, structures and activities of proteins." @default.
- W2078336233 created "2016-06-24" @default.
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- W2078336233 date "2013-11-01" @default.
- W2078336233 modified "2023-10-18" @default.
- W2078336233 title "Probing water micro-solvation in proteins by water catalysed proton-transfer tautomerism" @default.
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- W2078336233 doi "https://doi.org/10.1038/ncomms3611" @default.
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