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Related Concept Videos

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
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...
Protein Denaturation01:28

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

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NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
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Protein conformational disorder and enzyme catalysis.

Cindy Schulenburg1, Donald Hilvert

  • 1Laboratory of Organic Chemistry, ETH Zürich, 8093, Zürich, Switzerland.

Topics in Current Chemistry
|March 29, 2013
PubMed
Summary

Intrinsically unstructured proteins, lacking defined 3D structures, are vital for cellular signaling and regulation. Surprisingly, these disordered proteins can also perform enzyme catalysis, challenging traditional views of protein function.

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Last Updated: May 12, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Science

Background:

  • Intrinsically unstructured proteins (IUPs) are prevalent in nature despite lacking stable three-dimensional structures.
  • These proteins are critical for cellular processes, particularly in signaling and regulatory pathways.
  • The presence of disorder in enzymes challenges conventional understanding of protein structure-function relationships.

Purpose of the Study:

  • To review the properties and characteristics of disordered proteins.
  • To highlight enzymes that function effectively without defined structures.
  • To explore the implications of structural disorder for enzyme catalysis, efficiency, and evolution.

Main Methods:

  • Literature review of intrinsically unstructured proteins.
  • Analysis of enzymatic functions in disordered proteins.
  • Discussion of protein dynamics and its role in enzyme catalysis.

Main Results:

  • Disordered proteins are essential for key cellular functions like signaling and regulation.
  • Enzyme catalysis is shown to be compatible with significant structural disorder.
  • Protein dynamics plays a modulatory role in enzyme function.

Conclusions:

  • Structural disorder in proteins does not preclude essential biological functions, including catalysis.
  • Understanding protein dynamics is key to comprehending enzyme function.
  • The study of disordered proteins offers new perspectives on enzyme evolution and efficiency.