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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Tris(2-carboxyethyl)phosphine is an alternative reducing agent that is more stable and effective at low pH, but it is bulky and reduces cystines in folded proteins only slowly. [ 6 ] DTT's half-life is 40 hours at pH 6.5 and 1.4 hours at pH 8.5 and 20 °C; its half-life decreases further as temperature increases.
Denaturation is the process by which foods or liquids are made unpleasant or dangerous to consume; it is done by adding a substance known as a denaturant. Aversive agents —primarily bitterants and pungent agents —are often used to produce an unpleasant flavor.
A chaotropic agent is a molecule in water solution that can disrupt the hydrogen bonding network between water molecules (i.e. exerts chaotropic activity). This has an effect on the stability of the native state of other molecules in the solution, mainly macromolecules ( proteins , nucleic acids ) by weakening the hydrophobic effect .
There are many different families of chaperones; each family acts to aid protein folding in a different way. In bacteria like E. coli, many of these proteins are highly expressed under conditions of high stress, for example, when the bacterium is placed in high temperatures, thus heat shock protein chaperones are the most extensive.
The tertiary structure of the channel allows ions to flow through the hydrophobic plasma membrane. Connexons are an example of a homomultimeric protein composed of six identical connexins . A cluster of connexons forms the gap-junction in two neurons that transmit signals through an electrical synapse .
The post, which has now gained over 5.4 million views, was just one of many in his known series: “Things I would never do as a retired FBI agent.” Lazarus’ topic for the day was home DNA ...
Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GnHCl to gelatin and a mixture of thermally denatured protein from brain extract. . Greenstein (1938, 1939), however, appears to be the first to discover the high denaturing action of guanidinium halides and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin and other proteins as a ...