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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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Related Experiment Video

Updated: May 19, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein folding: a problem with multiple solutions.

Robert Paul Bywater1

  • 1Magdalen College, University of Oxford High Street, Oxford, UK. romeobravo@adelard.org.uk

Journal of Biomolecular Structure & Dynamics
|August 9, 2012
PubMed
Summary
This summary is machine-generated.

Protein structure prediction must account for proteins existing in multiple states. Key structural changes, including hydrogen bonding, hydrophobic contacts, and core packing, vary independently between conformers.

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Last Updated: May 19, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

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Published on: April 10, 2012

Interview: Protein Folding and Studies of Neurodegenerative Diseases
19:50

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Published on: July 16, 2008

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

Area of Science:

  • Biochemistry
  • Structural Biology
  • Computational Biology

Background:

  • Protein structure prediction aims to determine protein fold class and atomic resolution structures.
  • Sophisticated protein folding methods have achieved successes, but proteins can exist in multiple stable or metastable states.

Purpose of the Study:

  • To identify key structural changes during protein state transitions.
  • To analyze the independence of hydrogen bonding and hydrophobic interactions in protein conformational changes.
  • To investigate alterations in core packing and internal cavity volumes during protein folding.

Main Methods:

  • Analysis of structural changes in two-state protein systems.
  • Examination of hydrogen bonding patterns and hydrophobic contacts.
  • Assessment of core packing and internal cavity volumes.

Main Results:

  • Significant variations in hydrogen bonding and hydrophobic contacts were observed between protein conformers.
  • These interactions were found to operate largely independently.
  • Considerable changes in internal cavity volumes and core packing were identified in many cases.

Conclusions:

  • Protein structure prediction models must incorporate the possibility of multiple protein states.
  • Understanding the independent contributions of different interaction types is crucial for accurate prediction.
  • Fold-dependent mechanisms govern protein state switching, impacting structure prediction strategies.