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Issue 26, 2010
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Single-molecule, real-time measurement of enzyme kinetics by alternating-laser excitation fluorescence resonance energy transfer

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Abstract

Using a single-molecule fluorescence method uniquely suitable for binding assay, alternating-laser excitation fluorescence resonance energy transfer (ALEX-FRET), we accurately measured the cleavage rate of 8–17 deoxyribozyme, an RNA-cleaving enzyme, at the single-molecule level in real time with a minimum consumption of samples, i.e., at least three orders of magnitude smaller than used in the conventional ensemble FRET method.

Graphical abstract: Single-molecule, real-time measurement of enzyme kinetics by alternating-laser excitation fluorescence resonance energy transfer

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Publication details

The article was received on 08 Feb 2010, accepted on 13 May 2010 and first published on 01 Jun 2010


Article type: Communication
DOI: 10.1039/C002666B
Citation: Chem. Commun., 2010,46, 4683-4685
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    Single-molecule, real-time measurement of enzyme kinetics by alternating-laser excitation fluorescence resonance energy transfer

    N. K. Lee, H. R. Koh, K. Y. Han, J. Lee and S. K. Kim, Chem. Commun., 2010, 46, 4683
    DOI: 10.1039/C002666B

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