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Don’t FRET: Bimolecular Fluorescence Complementation Makes Visualizing Protein-Protein Interactions Easy

Posted by Guest Blogger on Aug 27, 2020 9:15:00 AM

This post was contributed by Patrick Miller-Rhodes from the University of Rochester Medical Center. 

You’ve probably heard of Forster Resonance Energy Transfer (FRET). Through the non-radiative transfer for energy between neighboring fluorophores, FRET can be used to detect the inter- and intramolecular interactions that underlie protein function. However, FRET experiments can be difficult to implement in practice because FRET depends on a number of hard-to-achieve factors. For example, FRET requires that fusion proteins be in close proximity and present in large enough quantities (and the correct stoichiometric ratios) to generate useable data. What’s more, measuring and quantifying FRET is often easier said than done.

Fortunately, a complementary method exists for visualizing protein-protein interactions (PPIs): Bimolecular Fluorescence Complementation (BiFC).

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Topics: Fluorescent Proteins, FRET

Genetically-encoded Sparse Cell Labeling - A SPARC of Innovation

Posted by Aliyah Weinstein on May 21, 2020 9:15:00 AM

Until recently, there were no completely genetic tools that would allow researchers to label just a fraction of a single genetically-defined subset of cells. By labeling fewer cells in a population, it’s easier to visualize individual/non-overlapping cells. While transgenic animals are commonly used to specifically manipulate a cell type of interest in an organism, all cells of that type are affected. Previous tools to overcome this restraint include an AAV-based sparse labeling system where a limiting amount of AAV are injected into the brain of Cre-expressing mice to trigger recombination and expression of a transgene (Lin et al., 2018). However, this system requires precise titration of the AAV. So far, tools to overcome this challenge in Drosophila require heat-shocking the system or using chemical inducers of gene expression (del Valle Rodríguez et al., 2011). 

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Topics: Fluorescent Proteins, Fluorescent Imaging

Chromoproteins: Colorful Proteins For Molecular Biology Experiments

Posted by Jennifer Tsang on Feb 4, 2020 9:15:00 AM

The ocean is full of striking visuals from fluorescent jellyfish, bioluminescent phytoplankton, and colorful corals, to name a few. What’s behind these sights are an abundance of biological molecules like chromoproteins, fluorescent proteins, and luminescent proteins. While fluorescent proteins and luminescence have been widely used in biological research for a long time, chromoproteins are just now being developed for a broad range of biological inquiries. 

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Topics: Fluorescent Proteins, Other Fluorescent Protein Tools

HA Frankenbody, a New Imaging Tool to Visualize Single Molecules and Nascent Peptides

Posted by Alyssa Cecchetelli on Oct 10, 2019 8:41:58 AM

Part stable scaffold, part epitope binding region, all fused to a fluorescent protein. “Frankenbody,” like the infamous frankenstein, was constructed by grafting different parts together. By combining two optimized elements of an antibody probe, scientists can now more easily visualize single molecules and newly formed proteins. 

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Topics: Fluorescent Proteins, Localization with Fluorescent Proteins

FlipGFP, a novel fluorescence protease reporter to study apoptosis

Posted by Alyssa Cecchetelli on May 21, 2019 8:10:19 AM

Apoptosis or “programmed cell death" plays a pivotal role in an array of biological processes including development, the immune system, and cell turnover. Apoptosis is a highly controlled process that is triggered by internal and external signals such as developmental cues and DNA damage. These signals activate a cascade of caspases, protease enzymes that cleave proteins. Executioner caspases are activated last in the cascade and are responsible for the degradation of over 600 cellular components ultimately leading to cell fragmentation and death (Elmore, 2007).

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Topics: Fluorescent Proteins, Other

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