Probing water micro-solvation in proteins by water catalysed proton-transfer tautomerism

Jiun-Yi Shen, Wei-Chih Chao, Chun Liu, Hsiao-An Pan, Hsiao-Ching Yang (), Chi-Lin Chen, Yi-Kang Lan, Li-Ju Lin, Jinn-Shyan Wang, Jyh-Feng Lu, Steven Chun-Wei Chou, Kuo-Chun Tang and Pi-Tai Chou ()
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Jiun-Yi Shen: Center for Emerging Material and Advanced Devices, National Taiwan University
Wei-Chih Chao: Center for Emerging Material and Advanced Devices, National Taiwan University
Chun Liu: Center for Emerging Material and Advanced Devices, National Taiwan University
Hsiao-An Pan: Center for Emerging Material and Advanced Devices, National Taiwan University
Hsiao-Ching Yang: Fu-Jen Catholic University
Chi-Lin Chen: Center for Emerging Material and Advanced Devices, National Taiwan University
Yi-Kang Lan: Fu-Jen Catholic University
Li-Ju Lin: School of Medicine, Fu-Jen Catholic University
Jinn-Shyan Wang: School of Medicine, Fu-Jen Catholic University
Jyh-Feng Lu: School of Medicine, Fu-Jen Catholic University
Steven Chun-Wei Chou: Center for Emerging Material and Advanced Devices, National Taiwan University
Kuo-Chun Tang: Center for Emerging Material and Advanced Devices, National Taiwan University
Pi-Tai Chou: Center for Emerging Material and Advanced Devices, National Taiwan University

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms3611

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