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Related Concept Videos

Activation and Inactivation of G Proteins01:22

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Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high...
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Green Fluorescent Protein-based Expression Screening of Membrane Proteins in Escherichia coli
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Fluorogen-activating proteins: beyond classical fluorescent proteins.

Shengnan Xu1, Hai-Yu Hu1,2

  • 1State Key Laboratory of Bioactive Substances and Function of Natural Medicine, Institute of Materia Medica, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100050, China.

Acta Pharmaceutica Sinica. B
|June 9, 2018
PubMed
Summary
This summary is machine-generated.

Fluorogen activating proteins (FAPs) enable real-time, noninvasive protein imaging in living cells. This technology offers high signal-to-noise ratios and multicolor labeling without washing steps.

Keywords:
Fluorescence imagingFluorogen activating proteinsFluorogensGenetically encoded sensorsMolecular imaging

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Imaging

Background:

  • Fluorescence imaging is crucial for monitoring protein dynamics in real-time.
  • Traditional fluorescent proteins (FPs) have limitations in specificity and require washing steps.
  • Fluorogen activating proteins (FAPs) and their probes offer an alternative imaging approach.

Purpose of the Study:

  • To review the discovery and development of FAP technology for protein imaging.
  • To discuss the design strategies for FAP fluorogens.
  • To highlight the applications and advancements of FAP technology in cellular labeling.

Main Methods:

  • Review of scientific literature on FAP discovery and development.
  • Analysis of FAP-fluorogen binding mechanisms.
  • Examination of FAP applications in multicolor live-cell imaging.

Main Results:

  • FAPs provide specific protein detection without requiring a washing step.
  • FAP technology enables high signal-to-noise ratio imaging in living cells.
  • Development of multicolor labeling systems using FAPs and various fluorogens.

Conclusions:

  • FAP technology represents a significant advancement in live-cell protein imaging.
  • The FAP system offers enhanced specificity, speed, and multiplexing capabilities.
  • Continued development of FAPs and fluorogens promises broader applications in biological research.