Related Experiment Video
Updated: Mar 18, 2026

Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions
Published on: January 30, 2018
Dynamical Structures of Hsp70 and Hsp70-Hsp40 Complexes
Thomas Reid Alderson1, Jin Hae Kim2, John Lute Markley2
1Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3TA, UK; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Molecular chaperones heat shock protein 70 kDa (Hsp70) and Hsp40 prevent toxic protein aggregation. Structural biology and nuclear magnetic resonance reveal how these proteins maintain cellular protein homeostasis.
Area of Science:
- Cellular Biology
- Structural Biology
- Biochemistry
Background:
- Protein misfolding and aggregation are implicated in various pathologies.
- Cellular protein homeostasis (proteostasis) relies on molecular chaperones for prevention and repair.
- Heat shock protein 70 kDa (Hsp70) and Hsp40 are key chaperones that bind misfolded proteins.
Purpose of the Study:
- To review the structural biology of Hsp70 and Hsp40-Hsp70 complexes.
- To examine the relationship between the structures, dynamics, and functions of these chaperones.
- To highlight the utility of nuclear magnetic resonance spectroscopy in studying chaperone mechanisms.
Main Methods:
- Review of existing literature on Hsp70 and Hsp40 structural biology.
- Analysis of structural and dynamic data for Hsp70 and Hsp40-Hsp70 complexes.
- Emphasis on nuclear magnetic resonance spectroscopy techniques.
Main Results:
- Detailed insights into the structural and dynamic properties of Hsp70 and Hsp40-Hsp70 complexes.
- Elucidation of how chaperone structure and dynamics influence their function in preventing protein aggregation.
- Demonstration of nuclear magnetic resonance spectroscopy's power in dissecting chaperone mechanisms.
Conclusions:
- Hsp70 and Hsp40 play critical roles in maintaining proteostasis by preventing toxic protein aggregation.
- Understanding the structural and dynamic basis of chaperone action is key to comprehending their function.
- Nuclear magnetic resonance spectroscopy is a powerful tool for advancing our knowledge of molecular chaperone mechanisms.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...

