chaperone

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chap·e·rone

(shap-ĕ-rōn),
1. A protein required for the proper folding and/or assembly of another protein or protein complex.
2. One who accompanies a physician during physical examination of a patient of the opposite gender (from the physician).
[Eng. escort, protector, fr. Fr. chaperon, hood, fr. chape, cape, fr. L.L. cappa, fr. L. caput, head]

chaperone

/chap·er·one/ (shap´er-ōn) someone or something that accompanies and oversees another.
molecular chaperone  any of a diverse group of proteins that oversee the correct intracellular folding and assembly of polypeptides without being components of the final structure.

chaperone

or

chaperon

(shăp′ə-rōn′)
n.
Any of a diverse group of proteins that assist macromolecules, such as proteins and nucleic acids, to assemble and fold into the proper three-dimensional structure as they are being synthesized. Also called molecular chaperone.

chap′er·on′age (-rō′nĭj) n.

chaperone

Cell biology
Any of a class of cytoplasmic proteins found in both prokaryotes and eukaryotes, which facilitate the correct assembly or disassembly of newly synthesised oligomeric protein complexes, participating in transmembrane targeting and protein folding.

Medspeak-UK
A person, generally employed by a medical doctor or (NHS) hospital trust, who stays with the patient while the doctor is examining a patient or performing a procedure.
 
Vox populi
A person who accompanies a child or adolescent under the age of majority (adulthood) during an event such as a date or a school dance.

chap·e·rone

(shap'ĕ-rōn)
1. A protein required for the proper folding and/or assembly of another protein or protein complex.
2. One who accompanies a physician during physical examination of a patient of the opposite gender (from that of the physician).
[Eng. escort, protector, fr. Fr. chaperon, hood, fr. chape, cape, fr. L.L. cappa, fr. L. caput, head]

chaperone

a PROTEIN MOLECULE which can assist in the folding, assembly or transport of other proteins in a CELL.

chaperone

a family of proteins that aid in the folding of target proteins.
References in periodicals archive ?
Cu transporters, chaperone proteins and carrier proteins make Cu available to the intricate network of biochemical systems.
Washington, Dec 4 (ANI): In a new study, scientists found that dynamic regulation of the chaperone protein Hsp27 is required to get rid of abnormally accumulating tau in the brains of mice genetically modified to develop the memory-choking tau tangles associated with Alzheimer's disease.
Hsf-1 is thought to be a master regulator that controls the amount of an entire family of molecular chaperone proteins that repair or degrade toxic misfolded proteins present in diseased cells.
These mechanisms include specialized agents that clear ROS, known as anti-oxidants, as well as specialized repair proteins, known as stress or chaperone proteins.
Among the most important components of the stress response is the production of molecular chaperone proteins that have the ability to refold a protein into a non-toxic shape or recruit other proteins that have the ability to "tag" the toxic protein for destruction.