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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.
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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...
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
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution00:52

¹H NMR of Conformationally Flexible Molecules: Temporal Resolution

At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...

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Related Experiment Video

Updated: May 16, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Conformational selection in substrate recognition by Hsp70 chaperones.

Moritz Marcinowski1, Mathias Rosam, Christine Seitz

  • 1Department Chemie, Technische Universität München, 85748 Garching, Germany.

Journal of Molecular Biology
|December 5, 2012
PubMed
Summary
This summary is machine-generated.

Heat shock proteins 70 (Hsp70s) are crucial for protein folding. This study reveals how Hsp70s bind client proteins, identifying specific binding sites and substrate conformations essential for interaction.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Heat shock proteins 70 (Hsp70s) function as molecular chaperones, essential for protein homeostasis.
  • Hsp70s bind to hydrophobic regions on substrate proteins to facilitate folding and assembly.
  • The precise mechanisms governing Hsp70 substrate specificity remain incompletely understood.

Purpose of the Study:

  • To elucidate the substrate binding sites and specificity of the endoplasmic reticulum-resident Hsp70, BiP.
  • To investigate the structural basis of Hsp70-substrate interactions.
  • To understand the role of substrate conformation in Hsp70 binding.

Main Methods:

  • In silico modeling and analysis.
  • In vitro biochemical assays.
  • Characterization of Hsp70-substrate complexes using a natural client protein.

Main Results:

  • Identified two mutually recognized binding sites on a natural client protein for Hsp70 BiP.
  • Demonstrated that an extended substrate conformation is critical for stable Hsp70-substrate complex formation.
  • Revealed significant plasticity within the Hsp70 substrate binding groove.

Conclusions:

  • The binding mechanism of Hsp70s involves specific recognition of extended substrate conformations.
  • The substrate binding groove of Hsp70s exhibits unexpected conformational flexibility.
  • The fundamental Hsp70 binding mechanism is conserved across different Hsp70 family members.