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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Molecular Chaperones and Protein Folding03:00

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Protein Folding01:25

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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
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Bacterial Protein Maturation01:26

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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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Related Experiment Video

Updated: Jan 5, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Protein folding while chaperone bound is dependent on weak interactions.

Kevin Wu1,2, Frederick Stull1,3,4, Changhan Lee1,3

  • 1Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI, 48109-1085, USA.

Nature Communications
|October 25, 2019
PubMed
Summary
This summary is machine-generated.

Chaperone proteins help other proteins fold. We found that while some chaperones allow client proteins to fold while bound, excessively strong binding inhibits this folding process.

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Area of Science:

  • Molecular biology
  • Protein folding
  • Biochemistry

Background:

  • Protein folding is essential for cellular function.
  • Chaperone proteins assist in protein folding.
  • It is generally assumed that client proteins fold after detaching from chaperones.

Purpose of the Study:

  • To investigate the relationship between chaperone-client binding strength and client protein folding.
  • To determine if tighter chaperone binding inhibits folding while chaperone-bound.

Main Methods:

  • Studied the ATP-independent chaperone Spy and its client protein SH3.
  • Manipulated the interaction strength between Spy and SH3.
  • Measured the folding rate of SH3 while bound to Spy.

Main Results:

  • The chaperone Spy allows client protein Im7 to fold while bound.
  • Strengthening the Spy-SH3 interaction significantly inhibits SH3 folding while bound.
  • Tighter binding between Spy and its client slows the client's folding rate.

Conclusions:

  • Efficient chaperone-mediated folding requires a balance between sufficient binding for mediation and avoiding overly tight interactions.
  • The strength of the chaperone-client interaction is a critical factor in chaperone-assisted folding.
  • Evolutionary pressures likely optimize chaperone-client interactions for efficient folding.