Guanidinium chloride

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Guanidinium chloride (GndCl) is one of the strongest denaturants used in physiochemical studies of protein folding. In 6 M GndCl all proteins with well ordered structure lose it, and most of them become randomly coiled, i.e. they do not contain any residual structure.

[edit] Historical Survey

Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GndCl 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 thiocynates in following the liberation of sulfhydryl groups in ovalbumin and few other proteins as a function of salt concentration.

[edit] References

1. Lapange, Savo (1978). Physicochemical aspects of protein denaturation. New York: Wiley. ISBN 0471034096.