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Related Concept Videos

Protein Folding01:22

Protein Folding

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

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
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...

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Related Experiment Video

Updated: May 14, 2026

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

Evolutionary optimization of protein folding.

Cédric Debès1, Minglei Wang, Gustavo Caetano-Anollés

  • 1Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.

Plos Computational Biology
|January 24, 2013
PubMed
Summary

Protein evolution has accelerated folding speeds over billions of years, with alpha-helices folding faster while beta-sheets have slowed. This optimization impacts protein structure and function.

Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • Proteins exhibit vast structural diversity shaped by evolution over 3.8 billion years.
  • The key drivers of protein structural evolution remain largely unknown.
  • Understanding protein evolution is crucial for deciphering cellular functions.

Purpose of the Study:

  • To investigate the relationship between protein evolution and protein folding speed.
  • To determine if evolutionary changes in protein structure correlate with changes in folding kinetics.
  • To explore the impact of secondary structure on protein folding speed over evolutionary time.

Main Methods:

  • Estimated folding times for current protein domains using size-modified contact order.
  • Mapped folding times onto an evolutionary timeline based on phylogenomic analysis of 989 genomes.

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

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Last Updated: May 14, 2026

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

Published on: July 25, 2013

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

  • Analyzed evolutionary trends in folding speed for alpha-helical and beta-sheet protein structures.

    • Main Results:

    • A general increase in protein folding speed was observed throughout evolution.
    • Ultra-fast folding proteins emerged relatively late in the evolutionary timeline.
    • Alpha-helical proteins trended towards faster folding, while beta-sheet proteins showed increased folding times in the last 1.5 billion years.

    Conclusions:

    • Fast and efficient protein folding has been a significant factor in shaping protein structural diversity.
    • Optimized folding kinetics may reduce protein aggregation, thereby enhancing cellular functions.
    • Secondary structure composition plays a critical role in the evolutionary trajectory of protein folding speed.