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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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...

Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

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Updated: Apr 7, 2026

Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Published on: April 25, 2021

Trace fluorescent labeling for protein crystallization.

Marc Pusey¹, Jorge Barcena¹, Michelle Morris¹

¹iXpressGenes Inc., 601 Genome Way, Huntsville, AL 35810, USA.

Acta Crystallographica. Section F, Structural Biology Communications

|July 7, 2015

Summary

This summary is machine-generated.

Trace fluorescent labeling aids protein crystallization screening without impacting results. This method enhances crystal visibility, even within precipitate, and identifies promising leads for optimization.

Keywords:

crystallization intensity screening trace fluorescence labeling

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Crystallization of Membrane Proteins in Lipidic Mesophases

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Published on: March 28, 2011

Area of Science:

Biochemistry
Structural Biology
Crystallography

Background:

Fluorescence is a valuable tool for protein crystallization.
Trace-labeling involves covalently attaching fluorescent probes to proteins.
High-quantum-yield, visible-wavelength probes are used at low concentrations (≤0.20%).

Purpose of the Study:

To evaluate the impact of trace fluorescent labeling on protein crystallization screening outcomes.
To assess if fluorescent labeling affects crystal nucleation or diffraction quality.
To explore additional benefits of fluorescence in crystallization screening.

Main Methods:

Proteins were covalently derivatized with fluorescent probes.
Labeled and unlabeled proteins were used in standard plate-screening experiments.
Crystals were identified by their bright fluorescence under illumination.

Main Results:

Trace fluorescent labeling did not alter crystallization screening outcomes compared to unlabeled proteins.
Crystals were clearly visualized, even when obscured by precipitate.
Approximately 30% of 'hidden' leads identified via fluorescence were optimized to crystals in a single pass.
Visible fluorescence allowed selection of probes to bypass interfering substances.

Conclusions:

Trace fluorescent labeling is a reliable method for protein crystallization screening.
Fluorescence enhances crystal detection and identification of potential leads.
This technique offers advantages over traditional methods, including improved visibility and identification of 'hidden' leads.