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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Evolution of New Traits in Microbes01:24

Evolution of New Traits in Microbes

Microorganisms evolve rapidly due to their large population sizes and short generation times, often exhibiting measurable changes within days under laboratory conditions. Natural selection acts on standing genetic variation, enabling the retention and amplification of beneficial traits that confer fitness advantages in changing environments.Adaptive Pigment Regulation in RhodobacterIn Rhodobacter, a genus of purple non-sulfur bacteria, light-harvesting pigments such as bacteriochlorophyll and...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
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.
In contrast, regions which code...

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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

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Published on: July 25, 2013

Reconstructing evolutionary adaptive paths for protein engineering.

Megan F Cole1, Vanessa E Cox, Kelsey L Gratton

  • 1School of Biology, Georgia Institute of Technology, Atlanta, GA, USA.

Methods in Molecular Biology (Clifton, N.J.)
|February 21, 2013
PubMed
Summary
This summary is machine-generated.

Reconstructing Evolutionary Adaptive Paths (REAP) is a protein engineering method using ancestral sequences to create functional enzyme variants. This low-throughput technique generates diverse, viable proteins efficiently for targeted trait selection.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Computational Biology

Background:

  • Enzyme functionality is crucial for various biological and industrial processes.
  • Protein engineering aims to enhance or modify enzyme properties.
  • Existing methods like DNA shuffling can be high-throughput but may lack focused diversity.

Purpose of the Study:

  • To introduce and describe the Reconstructing Evolutionary Adaptive Paths (REAP) method for protein engineering.
  • To highlight REAP's advantages in creating focused, highly functional enzyme variant libraries.
  • To explain the process of using ancestral sequences for directed gene mutations.

Main Methods:

  • Utilizes computational and theoretical aspects of protein engineering.
  • Employs ancestral protein sequences to guide gene mutations.
  • Generates a focused library of protein variants with high functionality.
  • Incorporates natural selection principles.

Main Results:

  • REAP creates libraries with diverse functionality among relatively few variants.
  • The method yields a high density of viable protein variants.
  • Enables targeted improvement of enzyme traits such as acid or thermostability.

Conclusions:

  • REAP offers an efficient, low-throughput approach to protein engineering.
  • The method effectively enhances enzyme functionality through directed evolution.
  • Assaying variants is essential to identify desired functional traits.