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Related Concept Videos

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...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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Updated: May 18, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
06:51

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

Published on: July 21, 2021

Chaperone discovery.

Shu Quan1, James C A Bardwell

  • 1Department of Molecular, Cellular, and Developmental Biology, Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, USA. shuquan@umich.edu

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|September 13, 2012
PubMed
Summary
This summary is machine-generated.

Molecular chaperones aid protein folding and refolding. This review explores traditional and novel methods for discovering these essential protein-folding factors.

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Published on: September 2, 2019

Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology

Background:

  • Molecular chaperones are crucial for protein folding and refolding.
  • The study of molecular chaperones spans over 35 years.
  • Understanding chaperone mechanisms is vital for cellular health.

Purpose of the Study:

  • To review traditional methods for identifying molecular chaperones.
  • To discuss the advantages and limitations of classical chaperone discovery techniques.
  • To highlight recent advancements and new avenues for chaperone discovery.

Main Methods:

  • Review of historical research and literature on molecular chaperone identification.
  • Analysis of established techniques for discovering protein-folding factors.
  • Exploration of emerging technologies like folding biosensors.

Main Results:

  • Traditional methods have successfully identified key molecular chaperones.
  • Classical discovery routes have inherent limitations.
  • New approaches offer enhanced capabilities for identifying novel chaperones.

Conclusions:

  • Diverse methods have contributed to our understanding of molecular chaperones.
  • Recent technological advances are paving the way for more efficient chaperone discovery.
  • Continued exploration of chaperone functions is essential for advancing protein science.