Abstract
When protein solutions are frozen, a relatively narrow proton magnetic resonance signal can be detected at −25 °. This signal is attributed to “bound” water. Low concentrations (ca. 1 m) of urea and certain substituted ureas alter this signal, increasing the observed line width markedly and increasing the area by 10%. Evidence is offered that this signal is still primarily from water protons. No urea resonances are observed. The changes in the water signal are thought to be caused by denaturation of the protein. Approximately 1 urea/10 amino acids is sufficient to cause 50% denaturation of bovine serum albumin in the frozen solution. The PMR results are most consistent with a weak binding mechanism for urea action.
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