She will be well enough chaperoned by her rector and his wife until her auntie arrives. The Dowager Countess was chaperoning her daughter to the ball and was keeping a closer eye on her than she had done at Lady Phillips's. She was forever being chaperoned about by her mother or some other elderly female relative, which was all very well for a new debutante but decidedly slow for a lady of twenty three. Large arrays of cylindrical structures and their chaperoning conduits and connectors were at once majestic yet stylized in design.Īnd so, for one reason and another, they walked on in silence, chaperoned by the voice of Mrs. You are not my chaperone and I am not some thirteen-year-old waiting for the chance to sneak off for a roll in the haymow with the boy from two farms over. So, with Caspar to chaperone them, they had crossed the streets of Haarlem at dusk. Reluctantly she permitted Dolley to join with other young people, chaperoned of course, in attending parties, picnics, jaunts into the country.īotticelli for me and the fattest whore in Florence, with plenty left over for her elephant of a mother to act as chaperone! Recent advances in single-molecule analysis have brought insights into structural heterogeneity of chaperones, folding intermediates and affinity of chaperones for unstructured and structured protein chains.īest we can tell, the original vector technology, as used by Grace, included some other exotic moleculethe French have named it Chaperone, because that is what Benoit Moreau called it. Bulk biochemical measurements have informed us on the protein folding efficiency, and prevention of aggregation when chaperones are present during protein folding. Various approaches have been applied to study the structure, dynamics and functioning of chaperones. Such proteins violate Anfinsen's dogma, requiring protein dynamics to fold correctly. However, some highly specific 'steric chaperones' do convey unique structural (steric) information onto proteins, which cannot be folded spontaneously. In this case, chaperones do not convey any additional steric information required for proteins to fold. It is for this reason that many chaperones, but by no means all, are heat shock proteins because the tendency to aggregate increases as proteins are denatured by stress.

One major function of chaperones is to prevent both newly synthesised polypeptide chains and assembled subunits from aggregating into nonfunctional structures. The first protein to be called a chaperone assists the assembly of nucleosomes from folded histones and DNA and such assembly chaperones, especially in the nucleus, are concerned with the assembly of folded subunits into oligomeric structures. The chaperones are concerned primarily with protein folding. Chaperones are present when the macromolecules perform their normal biological functions and have correctly completed the processes of folding and/or assembly. In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.

Spell chaperone or chaperon