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 ?
When cells are subject to ER stress, they try to rectify the problem by increasing the number of chaperone molecules and by increasing the size of the endoplasmic reticulum.
The very large quantity of HCV protein transcribed by the endoplasmic reticulum requires more chaperone molecules to accomplish this increased folding load.
Inside the cells of organisms as diverse as bacteria and people, chaperone molecules work in a variety of ways to keep proteins on a productive path.