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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

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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 Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Protein folding: adding a nucleus to guide helix docking reduces landscape roughness.

Beth G Wensley1, Lee Gyan Kwa, Sarah L Shammas

  • 1Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

Journal of Molecular Biology
|August 25, 2012
PubMed
Summary

Spectrin domains R16 and R17 exhibit slow folding due to a rough energy landscape. Substituting five residues alters their folding mechanism, enabling faster protein folding.

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Area of Science:

  • Protein folding dynamics
  • Biophysics
  • Spectrin domain structure

Background:

  • Spectrin domains R16 and R17 exhibit slow folding kinetics.
  • Their folding occurs over a rough energy landscape.
  • This contrasts with the faster folding of the homologue R15.

Purpose of the Study:

  • To investigate the folding mechanism of spectrin domains R16 and R17.
  • To identify key residues influencing folding landscape and kinetics.
  • To explore strategies for accelerating the folding of R16 and R17.

Main Methods:

  • Utilized site-directed mutagenesis to create variants of R16 and R17.
  • Investigated the effects of residue substitutions on folding pathways.
  • Analyzed changes in energy landscape roughness and folding rates.

Main Results:

  • Substitution of five key residues significantly altered the folding mechanism of R16 and R17.
  • These substitutions reduced the roughness of the energy landscape.
  • The modified domains demonstrated faster folding rates compared to wild-type.

Conclusions:

  • The folding mechanism of R16 and R17 can be modulated by specific residue changes.
  • Altering the energy landscape provides an alternative, faster folding route.
  • These findings offer insights into protein folding frustration and design.