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Related Concept Videos

Protein Folding01:25

Protein Folding

10.7K
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
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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Protein Folding01:22

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Overview
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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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Updated: Dec 28, 2025

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
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Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

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Using protein engineering to understand and modulate aggregation.

Jessica S Ebo1, Nicolas Guthertz1, Sheena E Radford1

  • 1Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK; School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.

Current Opinion in Structural Biology
|February 23, 2020
PubMed
Summary

Protein aggregation mechanisms are complex, influenced by various protein states and interactions. Advances in computational methods and protein engineering offer new ways to predict and control aggregation for disease and therapeutic applications.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Protein Science
  • Biotechnology

Background:

  • Protein aggregation is a complex process initiated by various protein states, posing challenges in understanding molecular mechanisms due to competing interactions influencing solubility and stability.
  • Diverse methods, including computational algorithms and deep mutational scanning, are employed to study protein aggregation.

Purpose of the Study:

  • To review recent advances in understanding and controlling protein aggregation.
  • To highlight the role of protein engineering and computational methods in this field.

Main Methods:

  • Review of computational algorithms for identifying aggregation-prone regions.
  • Discussion of deep mutational scanning for protein sequence analysis.
  • Focus on protein engineering strategies.

Main Results:

  • Recent advances integrate computational and experimental approaches to study protein aggregation.
  • Protein engineering combined with computational tools shows promise for predicting and controlling aggregation.

Conclusions:

  • Improved computational methods and protein engineering are key to understanding and manipulating protein aggregation.
  • These advancements are crucial for addressing protein aggregation in human diseases and for developing protein-based therapeutics.