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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.0K
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...
18.0K
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

22
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Protein Folding01:25

Protein Folding

8.1K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.1K
Structural Protein Function01:56

Structural Protein Function

27.7K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
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Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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Related Experiment Video

Updated: Jul 11, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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The Hsp70 and JDP proteins: Structure-function perspective on molecular chaperone activity.

Szymon J Ciesielski1, Cameron Young1, Elena J Ciesielska2

  • 1Department of Chemistry and Biochemistry, University of North Florida, Jacksonville, FL, United States.

The Enzymes
|November 9, 2023
PubMed
Summary
This summary is machine-generated.

Molecular chaperones like Hsp70 proteins and J-domain partners (JDPs) are crucial for maintaining protein structure and function. This review explores their structural roles in preventing protein misfolding and aggregation.

Keywords:
HSPAHsp40Hsp70J-domainJ-domain protein (JDP)Molecular chaperoneProtein Quality Control (PQC)Protein foldingProteostasis Network (PN)

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Intracellular Refolding Assay
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Intracellular Refolding Assay

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

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Related Experiment Videos

Last Updated: Jul 11, 2025

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

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Intracellular Refolding Assay
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Intracellular Refolding Assay

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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Structural Biology

Background:

  • Proteins require specific 3D structures for function but are prone to misfolding and aggregation due to stability/dynamics compromise.
  • Protein misfolding and aggregation are linked to cellular stress and inherent folding errors.
  • Molecular chaperones, particularly Hsp70s and their J-domain protein (JDP) partners, are essential for cellular proteome integrity.

Approach:

  • This review synthesizes current knowledge on the structural characteristics of Hsp70 chaperones.
  • It examines the structural features of J-domain proteins (JDPs).
  • The review focuses on the structural basis of Hsp70-JDP interactions and their functional implications.

Key Points:

  • Hsp70 chaperones and JDPs form essential complexes to assist protein folding.
  • Structural insights reveal how Hsp70-JDP interactions regulate chaperone activity.
  • Understanding these structures is key to comprehending cellular protein quality control.

Conclusions:

  • The structural interplay between Hsp70s and JDPs is fundamental for cellular protein homeostasis.
  • Further structural studies can elucidate mechanisms of chaperone-mediated protein folding and disease prevention.
  • This review provides a structural perspective on the Hsp70-JDP machinery in biological contexts.