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Related Concept Videos

Protein Folding01:22

Protein Folding

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Protein Folding01:25

Protein Folding

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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Protein and Protein Structure02:15

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: Jun 26, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

Strong eukaryotic IRESs have weak secondary structure.

Xuhua Xia1, Martin Holcik

  • 1Department of Biology and Center for Advanced Research in Environmental Genomics, University of Ottawa, Ottawa, Canada.

Plos One
|January 7, 2009
PubMed
Summary

Internal Ribosome Entry Sites (IRES) in yeast and fruit flies show that weaker secondary structures correlate with higher IRES activity. This suggests a shared mechanism for cap-independent translation initiation.

Area of Science:

  • Molecular Biology
  • Genetics

Background:

  • Eukaryotic Internal Ribosome Entry Sites (IRES) are crucial for cap-independent translation initiation.
  • The structural characteristics of IRES elements, particularly their secondary structure, are not fully understood.

Purpose of the Study:

  • To test the hypothesis that eukaryotic IRESs generally lack significant secondary structure.
  • To investigate the relationship between RNA secondary structure and IRES activity in yeast and fruit fly models.

Main Methods:

  • Calculated the Minimum Folding Energy (MFE) of 60-nucleotide RNA segments upstream of the initiation codon in yeast and fruit fly IRESs.
  • Assessed secondary structure stability using MFE and its reverse complement.
  • Correlated calculated structural stability with empirically determined IRES activity.

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

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Last Updated: Jun 26, 2026

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
11:44

Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities

Published on: October 2, 2018

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A Protocol for Computer-Based Protein Structure and Function Prediction

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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

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Main Results:

  • IRES activity in both yeast and fruit flies strongly correlates with RNA structural stability.
  • The highest IRES activity was observed in RNA segments exhibiting the weakest secondary structure.
  • A subset of eukaryotic IRESs demonstrates minimal secondary structure in their 5'-UTR sequences.

Conclusions:

  • The findings support the hypothesis that certain eukaryotic IRESs possess low secondary structure.
  • The consistent results between yeast and fruit fly suggest a conserved mechanism for cap-independent translation initiation.
  • This mechanism appears to rely on unstructured RNA segments within the 5'-UTR.