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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
Protein and Protein Structure02:15

Protein and Protein Structure

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.
A protein's shape is critical to its function. For example, an enzyme can...
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...

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Related Experiment Video

Updated: Jun 27, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
13:02

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

Published on: December 28, 2019

How does a knotted protein fold?

Anna L Mallam1

  • 1St John's College and University Chemical Laboratory, Cambridge, UK. alm38@cam.ac.uk

The FEBS Journal
|December 17, 2008
PubMed
Summary
This summary is machine-generated.

Discover how protein folding can create complex knots, challenging previous scientific assumptions. This review explores the mechanisms and implications of these unexpected protein structures.

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Related Experiment Videos

Last Updated: Jun 27, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
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Published on: December 28, 2019

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The protein-folding problem addresses how polypeptide chains attain functional 3D structures.
  • Protein knotting was previously considered biologically improbable.
  • Recent discoveries reveal naturally occurring knotted proteins.

Purpose of the Study:

  • To review progress in understanding the formation of knotted proteins.
  • To examine experimental and computational insights into protein knotting.
  • To discuss mechanisms and implications of complex protein topologies.

Main Methods:

  • Review of experimental studies on protein knot formation.
  • Analysis of computational simulations of protein folding.
  • Examination of existing models of protein folding mechanisms.

Main Results:

  • Knotted protein structures have been experimentally identified.
  • The formation of these knots challenges current folding models.
  • Insights into how nature encodes and manages protein knots have been gained.

Conclusions:

  • Knotted proteins represent a significant challenge to established protein-folding theories.
  • Understanding knotted protein formation provides crucial insights into the protein-folding puzzle.
  • Further research is needed to fully elucidate the mechanisms and biological roles of protein knots.