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Related Concept Videos

From DNA to Protein03:06

From DNA to Protein

The flow of genetic information in cells from DNA to mRNA to protein is described by the central dogma, which states that genes specify the sequence of mRNAs, which in turn specify the sequence of amino acids making up all proteins. The decoding of one molecule to another is performed by specific proteins and RNAs. Because the information stored in DNA is so central to cellular function, it makes intuitive sense that the cell would make mRNA copies of this information for protein synthesis...
Labeling DNA Probes03:31

Labeling DNA Probes

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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Reporter Genes02:11

Reporter Genes

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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Tagging and Fusion Proteins01:24

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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Related Experiment Video

Updated: May 28, 2026

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence
11:51

Engineering 'Golden' Fluorescence by Selective Pressure Incorporation of Non-canonical Amino Acids and Protein Analysis by Mass Spectrometry and Fluorescence

Published on: April 27, 2018

A genetically encoded fluorescent amino acid.

Daniel Summerer1, Shuo Chen, Ning Wu

  • 1Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, SR202, La Jolla, CA 92037, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 21, 2006
PubMed
Summary
This summary is machine-generated.

Researchers genetically encoded a fluorescent amino acid, dansylalanine, into proteins in yeast. This method allows for selective protein labeling, enabling studies of protein structure and function in vitro and in vivo.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Selective protein labeling is crucial for studying protein structure, dynamics, localization, and interactions.
  • Existing methods for introducing fluorophores can have limitations in specificity and efficiency.

Purpose of the Study:

  • To develop a strategy for the selective and efficient biosynthetic incorporation of a low-molecular-weight fluorophore into proteins at defined sites.
  • To demonstrate the utility of this method for monitoring protein unfolding.

Main Methods:

  • Genetically encoding the fluorescent amino acid dansylalanine in Saccharomyces cerevisiae using an amber nonsense codon and an orthogonal tRNA/aminoacyl-tRNA synthetase pair.
  • Site-specific incorporation of dansylalanine into human superoxide dismutase.
  • Monitoring protein unfolding using the environmentally sensitive dansylalanine fluorophore in the presence of guanidinium chloride.

Main Results:

  • Successful genetic encoding and site-specific incorporation of dansylalanine into proteins.
  • Demonstrated the use of dansylalanine to monitor the unfolding of human superoxide dismutase.
  • The incorporated fluorophore exhibited environmentally sensitive properties.

Conclusions:

  • The described strategy enables selective and efficient biosynthetic incorporation of fluorophores into proteins.
  • This approach facilitates biochemical and cellular studies of protein structure and function.
  • The method is potentially applicable to various fluorophores in both prokaryotic and eukaryotic systems.