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Related Concept Videos

Mutations01:35

Mutations

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Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...
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Point and Frameshift Mutations01:30

Point and Frameshift Mutations

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Point mutations are genetic alterations involving the change of a single nucleotide base pair in DNA. Depending on how the alteration affects protein synthesis, they can lead to various consequences.Point mutations fall into the following types:Silent mutations occur when a nucleotide change does not alter the amino acid sequence due to the redundancy of the genetic code. For instance, changing ACC to ACA still encodes threonine, leaving the protein function unaffected. This occurs because...
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Exon Recombination02:32

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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. 
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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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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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.
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Following the Dynamics of Structural Variants in Experimentally Evolved Populations
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Insertions and deletions in protein evolution and engineering.

Simone Savino1, Tom Desmet1, Jorick Franceus2

  • 1Centre for Synthetic Biology (CSB), Department of Biotechnology, Ghent University, Coupure Links 653, 9000 Ghent, Belgium.

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|June 23, 2022
PubMed
Summary

Insertions and deletions (indels) are crucial for protein evolution and engineering, offering significant biotechnological potential. This review emphasizes indels, exploring methods and structural impacts for enhanced protein design.

Keywords:
Directed evolutionEnzyme engineeringFrameshift mutationIndelLoop graftingPolymerase slippage

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Traditional protein studies focus on amino acid substitutions, neglecting insertions and deletions (indels).
  • Indels represent a major source of genetic variation with significant evolutionary impact.
  • Recent advances highlight the underappreciated role and potential of indels in protein science.

Purpose of the Study:

  • To review the evolutionary importance and biotechnological relevance of indels.
  • To provide a comprehensive overview of methods for incorporating indels into protein engineering.
  • To discuss the structural tolerance and functional implications of indels, including frameshift mutations.

Main Methods:

  • Literature review of protein evolution and engineering studies.
  • Analysis of methodologies for random, semi-rational, and computational indel incorporation.
  • Examination of structural and functional data related to indels in proteins.

Main Results:

  • Indels are evolutionarily significant and offer vast biotechnological potential.
  • Various strategies exist to integrate indels into protein engineering workflows.
  • Proteins exhibit structural tolerance to indels, which can even link functions of disparate proteins.

Conclusions:

  • Indels are a powerful, yet often overlooked, tool in protein engineering.
  • Understanding indel effects is key to unlocking novel protein functions and designs.
  • Frameshift mutations present intriguing possibilities for protein innovation.