Fluorescence correlation spectroscopy: molecular recognition at the single molecule level
Related Experiment Video
Updated: Oct 16, 2026

Dual-Color Fluorescence Cross-Correlation Spectroscopy to Study Protein-Protein Interaction and Protein Dynamics in Live Cells
Published on: December 11, 2021
E Van Craenenbroeck1, Y Engelborghs
1Laboratory of Biomolecular Dynamics, University of Leuven, Heverlee, Belgium.
Abstract:
Fluorescence correlation spectroscopy (FCS) is a fluorescence microscopy technique that allows the study of molecular interactions in extremely low volumes, at nanomolar concentrations, even when binding is not accompanied by a fluorescence change. It can be applied directly in living cells. FCS clearly considerably extends the possibilities of the classical techniques used in molecular recognition studies and can be considered to belong to a growing group of techniques that allow detection at the single molecule level. In this review, several applications of FCS, both in vitro and in vivo, will be discussed.
Related Concept Videos
Super-resolution Fluorescence Microscopy
Atomic Fluorescence Spectroscopy
Fluorescence and Phosphorescence: Instrumentation
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Confocal Fluorescence Microscopy

