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Related Concept Videos

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.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
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Conserved Binding Sites01:49

Conserved Binding Sites

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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...
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Gene Evolution - Fast or Slow?02:05

Gene Evolution - Fast or Slow?

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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.
In contrast, regions which code...
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Protein Folding01:25

Protein Folding

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
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Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
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Leaky Scanning02:28

Leaky Scanning

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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Related Experiment Video

Updated: Mar 5, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

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Stepwise Evolution of a Buried Inhibitor Peptide over 45 My.

Achala S Jayasena1, Mark F Fisher1, Jose L Panero2

  • 1School of Molecular Sciences & ARC Centre of Excellence in Plant Energy Biology, The University of Western Australia, Perth, Australia.

Molecular Biology and Evolution
|March 24, 2017
PubMed
Summary

Novel peptides can evolve within existing proteins over millions of years. This study traces the stepwise evolution of the SunFlower Trypsin Inhibitor-1 (SFTI-1) peptide within sunflower albumin precursors.

Keywords:
Asteraceaebiosynthesispeptideprotein evolutionsunflower

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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

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Related Experiment Videos

Last Updated: Mar 5, 2026

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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

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

Published on: July 25, 2013

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Area of Science:

  • Evolutionary Biology
  • Molecular Evolution
  • Biochemistry

Background:

  • De novo gene evolution and novel protein emergence are key to biodiversity.
  • Research on de novo evolution primarily focuses on transcripts, with limited understanding of biochemical steps and timelines for new protein evolution.
  • Sunflower Preproalbumin with SFTI-1 (PawS1) is unique, producing both albumin and the potent SunFlower Trypsin Inhibitor-1 (SFTI-1) peptide.

Purpose of the Study:

  • To elucidate the stepwise evolutionary pathway and timeline of the SFTI-1 inhibitor peptide.
  • To investigate how novel peptides can evolve within existing protein structures without de novo gene formation.
  • To understand the biochemical and temporal stages enabling a new peptide's functional specialization.

Main Methods:

  • Assembled seed transcriptomes from 110 sunflower relatives dated using a chronogram.
  • Analyzed genetic insertion events and subsequent molecular evolutionary stages.
  • Investigated peptide size expansion, cyclization, and functional specialization.

Main Results:

  • A genetic insertion event approximately 45 million years ago (Ma) introduced dual cleavage sites in albumin precursors, creating a buried macrocycle.
  • Peptide expansion and the incorporation of Cys residues around 34 Ma resulted in a bicyclic structure.
  • Functional specialization into a protease inhibitor occurred approximately 23 Ma, demonstrating evolution within a host protein.

Conclusions:

  • Novel peptides can evolve through gradual modification within existing, non-essential protein regions.
  • The evolution of SFTI-1 illustrates a mechanism for generating novel peptide function without de novo gene evolution.
  • This process occurred without compromising the original host protein's function.