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Related Concept Videos

Intermolecular Forces in Solutions02:28

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The formation of a solution is an example of a spontaneous process, a process that occurs under specified conditions without energy from some external source.
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Atoms and molecules interact through bonds (or forces): intramolecular and intermolecular. The forces are electrostatic as they arise from interactions (attractive or repulsive) between charged species (permanent, partial, or temporary charges) and exist with varying strengths between ions, polar, nonpolar, and neutral molecules. The different types of intermolecular forces are ion–dipole, dipole–dipole, hydrogen bonds, and dispersion; among these, dipole–dipole, hydrogen...
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Intermolecular forces (IMF) are electrostatic attractions arising from charge-charge interactions between molecules. The strength of the intermolecular force is influenced by the distance of separation between molecules. The forces significantly affect the interactions in solids and liquids, where the molecules are close together. In gases, IMFs become important only under high-pressure conditions (due to the proximity of gas molecules). Intermolecular forces dictate the physical properties of...
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Intermolecular forces are attractive forces that exist between molecules. They dictate several bulk properties, such as melting points, boiling points, and solubilities (miscibilities) of substances. Molar mass, molecular shape, and polarity affect the strength of different intermolecular forces, which influence the magnitude of physical properties across a family of molecules.
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Updated: Jan 24, 2026

Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology
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Exploring Biomolecular Interaction Between the Molecular Chaperone Hsp90 and Its Client Protein Kinase Cdc37 using Field-Effect Biosensing Technology

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Intermolecular Interactions between Hsp90 and Hsp70.

Shannon M Doyle1, Joel R Hoskins1, Andrea N Kravats1

  • 1Laboratory of Molecular Biology, National Cancer Institute,National Institutes of Health, Bethesda, MD 20892, USA.

Journal of Molecular Biology
|May 25, 2019
PubMed
Summary
This summary is machine-generated.

Heat shock proteins Hsp90 and Hsp70 directly interact in bacteria and yeast. This interaction, crucial for protein remodeling, is facilitated by J-proteins and occurs at specific sites on Hsp90 and Hsp70.

Keywords:
DnaJHsp40Hsp82HtpGSsa1

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Heat shock proteins (Hsp90 and Hsp70) maintain protein homeostasis and aid cellular recovery from stress.
  • These chaperones collaborate in protein remodeling and activation, forming complexes with adaptor proteins like Hop in eukaryotes.
  • In bacteria and yeast, Hsp90 and Hsp70 can interact directly, even without adaptor proteins.

Purpose of the Study:

  • To identify the specific interaction sites between Hsp90 and Hsp70 in bacteria (E. coli) and yeast.
  • To clarify whether previously identified residues mediate direct interaction or conformational changes.
  • To understand the role of J-proteins in mediating Hsp70-Hsp90 interactions.

Main Methods:

  • Crosslinking experiments were employed to pinpoint protein-protein interaction sites.
  • Studies were conducted in both Escherichia coli and yeast models.
  • The influence of ATP and J-proteins on the interaction was investigated.

Main Results:

  • Direct interaction was confirmed between a site in the middle domain of Hsp90 and the J-protein binding site of Hsp70.
  • This direct interaction occurs in both E. coli and yeast.
  • J-proteins promote Hsp70-Hsp90 interaction in an ATP-dependent manner, likely by inducing an ADP-bound Hsp70 conformation.

Conclusions:

  • The study precisely identifies the direct physical interaction sites between Hsp90 and Hsp70.
  • This finding elucidates the mechanism of chaperone collaboration in protein remodeling.
  • Understanding these interactions is key to comprehending cellular stress responses and protein quality control.