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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Hsp90 chaperones protein folding in vitro.
H Wiech1, J Buchner, R Zimmermann
1Zentrum Biochemie/Abteilung Biochemie II, Universität Göttingen, Germany.
Nature
|July 9, 1992
Summary
Heat-shock protein 90 (Hsp90) acts as a molecular chaperone, preventing protein aggregation and enhancing correct protein folding in vitro. This suggests a novel mechanism for Hsp90
Area of Science:
- Molecular biology
- Cellular stress response
Background:
- Heat-shock protein 90 (Hsp90) is abundant in eukaryotic cytosol.
- Hsp90 is involved in protein maturation, activity modulation, and transport.
- Hsp90's functions may rely on protein structure formation.
Purpose of the Study:
- To investigate Hsp90's role in protein folding in vitro.
- To determine if Hsp90 can influence the folding process and prevent aggregation.
Main Methods:
- In vitro experiments were conducted to assess Hsp90's effect on protein folding.
- Binding stoichiometry of Hsp90 to substrate proteins was analyzed.
- The influence of nucleoside triphosphates on Hsp90's action was examined.
Main Results:
- Hsp90 suppresses protein aggregate formation by binding to target proteins.
- A stoichiometry of one Hsp90 dimer to one or two substrate molecules was observed.
- The yield of correctly folded and functional protein significantly increased.
- Hsp90's action was independent of nucleoside triphosphates.
Conclusions:
- Hsp90 functions as a molecular chaperone that promotes correct protein folding and prevents aggregation.
- Hsp90 may employ a novel mechanism for assisting protein folding in vivo, independent of nucleoside triphosphates.
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