ArticleBiophysical journal2012
Factors affecting the quantification of biomolecular interactions by fluorescence cross-correlation spectroscopy.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 107 citations in OpenAlex.
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- Cell cycle-dependent binding between Cyclin B1 and Cdk1 revealed by time-resolved fluorescence correlation spectroscopy.Open biology · 2022Article
- Novel Tools to Measure Single Molecules Colocalization in Fluorescence Nanoscopy by Image Cross Correlation Spectroscopy.Nanomaterials (Basel, Switzerland) · 2022Article
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- Multicolor fluorescence fluctuation spectroscopy in living cells via spectral detection.eLife · 2021Article
- Integrin intra-heterodimer affinity inversely correlates with integrin activatability.Cell reports · 2021Article
- Empirical Bayes method using surrounding pixel information for number and brightness analysis.Biophysical journal · 2021Article
- Simultaneous spatiotemporal super-resolution and multi-parametric fluorescence microscopy.Nature communications · 2021Article
- Measuring Nanoscale Distances by Structured Illumination Microscopy and Image Cross-Correlation Spectroscopy (SIM-ICCS).Sensors (Basel, Switzerland) · 2021Article
- Wnt3 Is Lipidated at Conserved Cysteine and Serine Residues in Zebrafish Neural Tissue.Frontiers in cell and developmental biology · 2021Article
- Number and Brightness Analysis: Visualization of Protein Oligomeric State in Living Cells.Advances in experimental medicine and biology · 2021Article
- Article
- Influence of FRET and fluorescent protein maturation on the quantification of binding affinity with dual-channel fluorescence cross-correlation spectroscopy.Biomedical optics express · 2020Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fluorescence cross-correlation spectroscopy (FCCS) is used to determine interactions and dissociation constants (K(d)s) of biomolecules. The determination of a K(d) depends on the accurate measurement of the auto- and cross-correlation function (ACF and CCF) amplitudes. In the case of complete binding, the ratio of the CCF/ACF amplitudes is expected to be 1. However, measurements performed on tandem fluorescent proteins (FPs), in which two different FPs are linked, yield CCF/ACF amplitude ratios of ~0.5 or less for different FCCS schemes. We use single wavelength FCCS and pulsed interleaved excitation FCCS to measure various tandem FPs constituted of different red and green FPs and determine the causes for this suboptimal ratio. The main causes for the reduced CCF/ACF amplitude ratio are differences in observation volumes for the different labels, the existence of dark FPs due to maturation problems, photobleaching, and to a lesser extent Förster (or fluorescence) resonance energy transfer between the labels. We deduce the fraction of nonfluorescent proteins for EGFP, mRFP, and mCherry as well as the differences in observation volumes. We use this information to correct FCCS measurements of the interaction of Cdc42, a small Rho-GTPase, with its effector IQGAP1 in live cell measurements to obtain a label-independent value for the K(d).
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