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Proteomics01:33

Proteomics

7.5K
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.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
7.5K
Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

6.4K
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: Apr 27, 2026

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
10:32

Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

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Tissue-specific proteome tagging: an orthogonal approach.

Adrienne L Snyder1, Eric M Brustad

  • 1Department of Chemistry, Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, 125 South Road, Chapel Hill, NC 27599 (USA).

Chembiochem : a European Journal of Chemical Biology
|July 4, 2014
PubMed
Summary

Researchers developed a versatile method to incorporate a novel cyclopropene amino acid into proteins using sense codons. This technique allows for targeted protein labeling within specific tissues through selective gene expression.

Keywords:
bio-orthogonal chemistrycycloadditiongenetic code expansionproteomicssynthetases

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Biology

Background:

  • The proteome is a complex system of proteins.
  • Targeted protein modification is crucial for biological research.
  • Current methods for protein labeling have limitations.

Purpose of the Study:

  • To develop a versatile method for incorporating a novel amino acid into the proteome.
  • To enable selective protein labeling in response to sense codons.
  • To achieve tissue-specific protein incorporation using orthogonal tRNA synthetases.

Main Methods:

  • Development of a novel 1,3-disubstituted cyclopropene amino acid.
  • Utilizing sense codons for amino acid incorporation into the proteome.
  • Employing orthogonal tRNA synthetases for targeted expression.
  • Implementing cell-selective promoters for tissue-specific control.

Main Results:

  • Successful incorporation of the cyclopropene amino acid into the proteome.
  • Demonstrated versatility in response to various sense codons.
  • Achieved confinement of incorporation to specific tissues via selective promoters.
  • Enabled subsequent labeling of the incorporated amino acid.

Conclusions:

  • A versatile method for proteome modification using a novel cyclopropene amino acid has been established.
  • The method allows for controlled and targeted protein labeling.
  • This approach offers potential for advanced biological studies and therapeutic applications.