Abstract
MUCH is known about the action of urea on proteins; the mechanism, however, is not understood. The long-accepted hydrogen-bond mechanism, once deemed quantitatively unsatisfactory1 but never tried seriously, is shown here to be erroneous on various theoretical and experimental grounds2,3. The alternatives in terms of the hydrophobic bond theories4–6 are stimulating but not fully consistent with the evidence: they are too arbitrary in that they do not take into account some important properties of urea and ignore the significant facts1,7,8 which are known about the action of urea and which cannot be in the domain of the hydrophobic forces alone. In all the previous studies no attention was paid to urea itself and to the polar properties which are obvious in the structure of the urea molecule and presumably fundamental to its mode of action. This communication aims at postulating and describing the urea cation, a zwitterion with a positive head charge.
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COLACICCO, G. Urea Cation in the Mechanism of Denaturation of Proteins. Nature 198, 583–584 (1963). https://doi.org/10.1038/198583a0
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DOI: https://doi.org/10.1038/198583a0
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