See beyond Structure with Fluorescence Correlation Spectroscopy

FCS allows for the analysis of concentrations and mobility of fluorescently labeled “particles” such as DNA, proteins, and ribosomes. Compared to other techniques that are commonly used for measuring these parameters, such as fluorescence recovery after photobleaching (FRAP), FCS requires lower laser power, so is less damaging to the sample, and importantly provides access to information about sub-populations, rather than an ensemble average over multiple populations or compartments.

- Access to data that is otherwise not obtainable
- Data on molecular level
- Identification of specific sub-populations of one labeled particle

FCCS allows for the measurement of dynamic co-localization, molecular interactions, and enzymatic reactions. Compared to common methods for assessing co-localization, such as fluorescence resonance energy transfer (FRET), interactions that occur at greater distances than are required for FRET (> 10 nm) can be measured, and there is greater freedom in fluorophore selection. Additionally, FCCS can easily be used to examine interactions between fast moving particles, which can be challenging with FRET as it is better suited for slower moving or static structures.

- Can be used for vesicle transport, assembly, and disassembly
- Large molecules and complexes: interaction even at > 10 nm distances
- FSCS: spectral cross-correlation spectroscopy with 32 channel GaAsP can provide additional information