Molecular chaperone
Molecular Chaperone
Molecular chaperones (pronunciation: mo-le-cu-lar chap-er-ones) are a class of proteins that assist in the folding, assembly, and disassembly of other macromolecular structures, particularly proteins. The term "chaperone" refers to the proteins' ability to guard and guide the target proteins to their correct three-dimensional structure, similar to how a human chaperone would guide or assist a person.
Etymology
The term "molecular chaperone" was first used in the 1980s. The name is derived from the French word "chaperon," which means "hood," originally referring to a type of protective headgear. In a biological context, the term was used metaphorically to describe the protective role these proteins play in assisting other proteins to achieve their correct structure.
Function
Molecular chaperones are involved in various cellular processes, including protein folding, the assembly of multi-protein complexes, and the transport of proteins across cellular membranes. They ensure that proteins fold into their correct shape and prevent misfolding and aggregation, which can lead to diseases such as Alzheimer's disease and Parkinson's disease.
Types
There are several types of molecular chaperones, including heat shock proteins, chaperonins, and co-chaperones. Each type has a specific function and operates in different cellular compartments.
Related Terms
- Protein folding: The process by which a protein structure assumes its functional shape or conformation.
- Protein aggregation: The biological phenomenon where misfolded proteins aggregate (i.e., accumulate and clump together) in cells.
- Neurodegenerative diseases: A range of conditions which primarily affect the neurons in the human brain.
External links
- Medical encyclopedia article on Molecular chaperone
- Wikipedia's article - Molecular chaperone
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