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Molecular Chaperones and Protein Folding

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...

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Updated: Mar 22, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

Published on: January 20, 2023

Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function.

Parul Mishra¹, Julia M Flynn¹, Tyler N Starr²

¹Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.

|April 13, 2016

Summary

Investigating the Hsp90 chaperone

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Last Updated: Mar 22, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

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Published on: January 20, 2023

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

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Published on: November 29, 2013

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

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Published on: July 21, 2021

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Heat shock protein 90 (Hsp90) is a crucial chaperone protein.
It facilitates the maturation of numerous signaling proteins in eukaryotic cells.
Understanding Hsp90's mechanism is vital for cellular regulation.

Purpose of the Study:

To elucidate the functional mechanism of the Hsp90 chaperone.
To analyze the impact of mutations within the ATPase domain on Hsp90 function.
To investigate client-specific chaperone mechanisms.

Main Methods:

Systematic analysis of all individual amino acid changes in the Hsp90 ATPase domain.
Assessing the effects of these mutations on yeast growth rate.
Biochemical analyses of Hsp90 mutants using v-src and glucocorticoid receptor (GR) as clients.

Main Results:

Mutation sensitivity correlated with proximity to ATP phosphates, revealing physical constraints.
Distinct effects of nine Hsp90 mutations on v-src and GR activation were observed.
Evidence suggests Hsp90 employs different mechanisms for distinct client proteins.

Conclusions:

ATPase-driven conformational changes impose stringent constraints on Hsp90.
Hsp90 exhibits client-specific chaperone mechanisms.
Findings support the development of targeted Hsp90 inhibitors.