Chaperone molecules chemical chaperones

The term chemical chaperone has been proposed to describe small molecules such as glycerol, dimethylsulfoxide, and trimethylamine N-oxide that act as protein-stabilizing agents. This terminology is unfortunate and confuses students, because proteins are also chemicals. This term should be replaced by the term kosmotrope that physical chemists use to describe small molecules that stabilise proteins. 

While it s clear that the body would not work properly without a prescribed amount of a select group of metals, some metals are indeed toxic to the body. Even for the metals your body needs, too much is not a good thing. Since metals are elements (the building blocks of all chemical compounds), as basic components of the Earth they cannot be broken down (like proteins and fats can, for instance). Thus your body takes great care to shepherd these potentially toxic materials to their proper destinations inside cells. As with copper, many other metals are escorted around by protective, chaperone-like molecules. 

One of the most important aspects of protein synthesis is the folding of polypeptides into their biologically active conformations. Despite decades of investigation into the physical and chemical properties of polypeptide chains, the mechanism by which a primary sequence dictates the molecule s final conformation is unresolved. It has become increasingly clear that many proteins require molecular chaperones to fold into their final three-dimensional conformations. Protein mis-folding is now known to be an important feature of several human diseases, including Alzheimer s disease and Creutzfeld-Jacob disease. 

It is noted that the theory does not envisage the existence of atoms or radicals intermediate between reactant and product, strongly bound to the surface. By physical forces the catalyst atoms attract various parts of the reactant molecule, and thereby enable it to form new bonds internally or with a neighboring reactant molecule, but they do not at any stage form chemical bonds with these parts. The function of the catalyst is to guide or chaperone rather than to participate, and Balandin has stated (8)The multiplet theory has always emphasized that, on the multiplet, only a deformation occurs, and this only in the limit becomes a dissociation into radicals, bound to the surface. Chemisorp-... 

For chemical reactions in solution, the solvent plays an important role in the elementary processes of bond making and breaking. For example, it may enhance bond formation by trapping reactive species in a solvent cage on the time-scale of the reaction it also may act as a chaperone that stabilizes energetic species. One of the most studied reactions in the condensed phase is that of dissociation of neutral iodine molecules most recently, it has been studied using ultrafast lasers to investigate its femtosecond dynamics. 

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