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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.
The...
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Molecular Chaperones and Protein Folding03:00

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The Equilibrium Binding Constant and Binding Strength02:18

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Updated: Jan 22, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

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Dynamic Aha1 co-chaperone binding to human Hsp90.

Javier Oroz1,2, Laura J Blair3, Markus Zweckstetter1,4

  • 1Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Göttingen, Germany.

Protein Science : a Publication of the Protein Society
|July 13, 2019
PubMed
Summary

The heat shock protein 90 (Hsp90) chaperone complex structure was determined using NMR spectroscopy. This reveals how the co-chaperone Aha1 regulates Hsp90

Keywords:
Aha1Hsp90allosteryco-chaperonestructure

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial molecular chaperone involved in protein homeostasis.
  • Hsp90 function relies on allosteric regulation of its ATPase activity and client protein binding.
  • The co-chaperone activator of Hsp90 ATPase 1 (Aha1) is a key stimulator of Hsp90's ATPase activity in eukaryotes.

Purpose of the Study:

  • To elucidate the solution structure of the human Hsp90/Aha1 complex.
  • To understand the mechanism by which Aha1 regulates Hsp90's ATPase activity.
  • To characterize the dynamic interactions within the Hsp90/Aha1 complex.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the structure of the Hsp90/Aha1 complex in solution.
  • The study focused on the unmodified human Hsp90/Aha1 complex.
  • Analysis of the complex's formation and conformational states in the absence of nucleotide.

Main Results:

  • The 214-kDa Hsp90/Aha1 complex was characterized in solution, revealing a two-step binding mechanism.
  • The complex was observed to adopt multiple conformations in the absence of nucleotide.
  • Aha1 binding induces significant structural alterations near Hsp90's nucleotide-binding site.

Conclusions:

  • The study provides novel insights into the structural dynamics of the Hsp90/Aha1 complex.
  • Aha1's role in enhancing Hsp90 ATPase activity is structurally explained by its induction of changes near the nucleotide-binding site.
  • Characterizing dynamic chaperone structures in solution is essential for understanding their function.