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a Related Biological Terms:

chalone

An inhibitory hormone.

channel former

A structure in a membrane that, without itself moving, allows passive diffusion of ions across the membrane.

chaotropic agent

A solute that disrupts the structure of the bulk water phase and, in so doing, changes the solubility and stability properties of other solutes, such as proteins.

chaperone

(see chaperone machine; RNA chaperone)

chaperone machine

A multicomponent system that ensures the proper folding of nascent proteins or their intracellular transport following synthesis; components include chaperones (eukaryotes) or chaperonins (from prokaryotes, mitochondria and plasmids), which bind to unfolded proteins; also peptidyl proline isomerases and heat-shock proteins, which can serve various ancillary functions. (see also RNA chaperone)Burston, S.G. and Clarke, A.R. (1995) Essays Biochem. 29, 125-136; Hendrick, J.P. and Hartl, F.-U. (1995) FASEB J. 9, 1559-1569; Ptitsyn, O.B. (1996) FASEB J. 10, 3-4; Hartl, F.-U. (1996) Nature (London) 381, 571-580

chaperonin

(see chaperone machine)

charge

In chemistry, the integral sum of positive and negative particles that make up a species, a cation if the charge is positive, an anion, if the charge is negative. In biochemistry, the loading of a binding site with its intended ligand, e.g. the appropriate amino acid bound to its tRNA; in cell biology, essentially as in biochemistry, but on a macromolecular level, e.g. the charging of a liposome with material for transport cross a cell membrane. Related service: cell line development

charge accumulator model

A conceptualization of the mechanism of the water-splitting enzyme of photosynthesis in which four electrons are sequentially removed from the manganese centre, enabling it to oxidize water to molecular oxygen.

charge ladder

A series of elution peaks seen upon capillary electrophoresis of modified versions of a protein that vary only in their electrostatic charge. (see also electrophoresis)Gao, J., Gomez, F.A., Harter, R. and Whitesides, G.M. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 12027-12030

charge relay system

A tautomeric form of a protein in which a formal charge on one dissociating group is moved to another in the same protein. In serine proteinases, for example, an internal αgamma-) carboxylate is partially protonated by bridging via an imidazole to an active-site nucleophile, often a serine hydroxy or cysteine thiol group, leaving the nucleophile with a negative charge and making it more reactive in its attack upon a substrate molecule. This group of residues is termed the catalytic triad. Learn more about amino acid chart.

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