New Fluorescence Technique For Ultra-Sensitive Enzyme Characterization Developed - Screening Catalytic Activity At The Single-Molecule Level

New fluorescence technique for ultra-sensitive enzyme characterization developed - Screening catalytic activity at the single-molecule level

Enzymes are characterized by and valued for their ability to catalyze a wide range of chemical reactions. Consequently, precise analytical techniques for monitoring enzyme functions are indispensable tools for the understanding of biological phenomena at the molecular level, and for the development of new pharmaceuticals. A research team at the Max Planck Institute for Biophysical Chemistry in Gttingen, Germany, headed by the Nobel laureate Manfred Eigen, published two articles in PNAS (Proceedings of theNational Academy of Sciences) introducing dual-color fluorescence cross-correlation spectroscopy as a new method for an ultra-sensitive characterization of enzyme activity (PNAS 95:1416-1420, abstract: http://www.pnas.org/cgi/content/abstract/95/4/1416) and demonstrating its potential for high throughput screening (PNAS 95:1421-1426, abstract: http://www.pnas.org/cgi/content/abstract/95/4/1421).

In recent years, fluorescence correlation spectroscopy (FCS) has become an attractive analytical tool for the investigation of biomolecular processes. Due to the interplay of modern confocal optics, new dyes as efficient fluorescent probes, sensitive photodetectors, and fast data processing, FCS allows the observation of the dynamics of single molecules in real time while they pass an open volume element of about one femtoliter, i.e. only the size of a common bacterial cell. This method was invented and worked out by groups at the Cornell University, Ithaca, at the Karolinska Institute, Stockholm, and at the Max Planck Institute, Gttingen; nowadays it has

Contact: Ulrich Kettling, Andre Koltermann
ukettli@gwdg.de, akolter@gwdg.de

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