Abstract
The denaturing effect of urea on protein molecules can be attributed to its influence on the structure of the hydrate layer, which surrounds and stabilizes the helical protein strand [1]. Urea has a very large capacity for hydrogen-bond formation and it is apparently for this reason that aqueous urea solutions have a number of unusual properties. Thus, for example, the solubility of urea in water is exceptionally high, reaching 20 M at 25°C; there are data indicating that aqueous urea solutions are close to ideal at all concentrations. The presence of urea in water increases the solubility of all hydrocarbons except methane and ethane and weakens the hydrophobic bonds in proteins.
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