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Related Concept Videos

Reporter Genes02:11

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Reporter genes are a type of protein-coding gene that are often tagged to a gene of interest. Once inside a target cell, reporter genes usually produce visually identifiable characteristics like fluorescence and luminescence when expressed along with the gene of interest. Thus, reporter genes “report” the presence or absence of genes of interest in an organism, determine the gene expression pattern, or track the physical location of a DNA segment or protein in the cell.
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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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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
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Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
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DNA probes are fragments of DNA labeled with a reporter tag to enable their detection or purification. The resulting labeled DNA probes can then hybridize to target nucleic acid sequences through complementary base-pairing, and may be used to recover or identify these regions.
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The number of nuclear spins aligned in the lower energy state is slightly greater than those in the higher energy state. In the presence of an external magnetic field, as the spins precess at the Larmor frequency, the excess population results in a net magnetization oriented along the z axis. When a pulse or a short burst of radio waves at the Larmor frequency is applied along the x axis, the coupling of frequencies causes resonance and flips the nuclear spins of the excess population from the...
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Multiple paramagnetic effects through a tagged reporter protein.

Aldo R Camacho-Zarco1, Francesca Munari, Melanie Wegstroth

  • 1Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen (Germany); German Center for Neurodegenerative Diseases (DZNE), Göttingen (Germany); Center for the Molecular Physiology of the Brain, University Medical Center, Göttingen (Germany).

Angewandte Chemie (International Ed. in English)
|October 9, 2014
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel method using a reporter protein to transfer paramagnetic information, enabling detailed structural and dynamic studies of large biomolecules. This technique enhances the analysis of high-molecular-weight proteins with unknown 3D structures.

Keywords:
NMR spectroscopylanthanoidsparamagnetismproteinsstructural biology

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Area of Science:

  • Biochemistry and structural biology
  • Biophysics

Background:

  • Paramagnetic effects offer valuable insights into biomolecular structure and dynamics.
  • Traditional methods for obtaining this information can be challenging for large or complex proteins.

Purpose of the Study:

  • To develop an innovative method for acquiring paramagnetic restraints and residual dipolar couplings.
  • To enable structural and dynamic characterization of high-molecular-weight proteins with previously unknown 3D structures.

Main Methods:

  • A novel approach was developed where a lanthanoid tag is attached to a "reporter" protein, not directly to the target protein.
  • The reporter protein binds to the target, transmitting paramagnetic information.
  • Independent molecular alignments were utilized to generate restraints.

Main Results:

  • The method successfully allows access to a large number of paramagnetic restraints.
  • Residual dipolar couplings were obtained from independent molecular alignments.
  • This approach is effective for high-molecular-weight proteins with unknown 3D structures.

Conclusions:

  • The developed method provides a powerful new tool for biomolecular structural and dynamic studies.
  • It overcomes limitations associated with directly tagging large proteins.
  • This technique facilitates the structural elucidation of challenging protein targets.