Jump to main content
Jump to site search
Access to RSC content Close the message box

Continue to access RSC content when you are not at your institution. Follow our step-by-step guide.


Issue 26, 2010
Previous Article Next Article

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

Author affiliations

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

Back to tab navigation

Supplementary files

Additions and corrections

Article information


Submitted
08 Feb 2010
Accepted
13 May 2010
First published
01 Jun 2010

Chem. Commun., 2010,46, 4683-4685
Article type
Communication

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

Social activity

Search articles by author

Spotlight

Advertisements