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Related Concept Videos

Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
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Gene Evolution - Fast or Slow?02:05

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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...
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Conservation of Protein Domains Over Different Proteins02:26

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Related Experiment Video

Updated: Jun 13, 2026

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers
10:41

Identifying Amino Acid Overproducers Using Rare-Codon-Rich Markers

Published on: June 24, 2019

Protein evolution via amino acid and codon elimination.

Lise Goltermann1, Marie Sofie Yoo Larsen, Rajat Banerjee

  • 1Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen, Denmark.

Plos One
|May 4, 2010
PubMed
Summary

Researchers engineered active green fluorescent protein (GFP) variants lacking phenylalanine residues using a novel protein evolution strategy. This method simplifies protein design and expands possibilities for synthetic biology applications.

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Area of Science:

  • Protein engineering
  • Synthetic biology
  • Biochemistry

Background:

  • Amino acid mutagenesis is key for biological insight but risks protein misfolding.
  • Library size increases exponentially with randomized residues, limiting complexity.
  • Current methods restrict randomization to few amino acids.

Purpose of the Study:

  • To develop a strategy for creating simplified, native-like polypeptides with reduced genetic codes.
  • To engineer active green fluorescent protein (GFP) variants lacking specific amino acids.
  • To expand the functional repertoire of uniquely labeled proteins for synthetic biology.

Main Methods:

  • A sequential mutagenesis scheme combined with stabilizing mutations, chaperone complementation, and reduced expression temperature.
  • Elimination of phenylalanine (Phe) residues from GFP through stepwise substitution and screening.
  • Combinatorial re-introduction of essential Phe residues to restore protein activity.

Main Results:

  • Active GFP variants with zero, two, and three Phe residues were successfully generated.
  • Engineered GFPs retained progenitor-like fluorescence spectra but showed temperature-sensitive folding and reduced stability.
  • The strategy enabled the creation of simplified, functional proteins through targeted amino acid elimination.

Conclusions:

  • The study provides strategies for designing novel GFP reporters.
  • The approach facilitates engineering active proteins lacking specific amino acids.
  • This work is a key step towards expanding the functional repertoire of uniquely labeled proteins in synthetic biology.