molecular chaperone
Sign in to saveAlso known as chaperones, chaperone, chaperone protein
proteins assisting in protein folding
Research
100,035 papers- Molecular chaperone functions in protein folding and proteostasis.Annual review of biochemistry · 2013
- Chaperone therapy for molecular pathology in lysosomal diseases.Brain & development · 2021
- Involvement of molecular chaperone in protein-misfolding brain diseases.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022
- Calnexin, More Than Just a Molecular Chaperone.Cells · 2023
- Molecular Chaperone HSP70 and Key Regulators of Apoptosis - A Review.Current molecular medicine · 2019
via PubMed
~13 min read
Encyclopedic overview
A top-view of the GroES/GroEL bacterial chaperone complex model In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation. Chaperones are also involved in the translocation of proteins for proteolysis.
The first molecular chaperones discovered were a type of assembly chaperones which assist in the assembly of nucleosomes from folded histones and DNA. One major function of molecular chaperones is to prevent the aggregation of misfolded proteins, thus many chaperone proteins are classified as heat shock proteins, as the tendency for protein aggregation is increased by heat stress.
Excerpted from Wikipedia’s “molecular chaperone” article, available under the CC BY-SA 4.0 licence.