Guanidinium chloride
Encyclopedia
Guanidinium chloride or guanidine hydrochloride, usually abbreviated GdmCl and sometimes GndCl or GuHCl, is the hydrochloride
salt of guanidine
.
s used in physiochemical studies of protein folding
. In 6 molar guanidinium chloride solution, all protein
s with well ordered structure lose it, and most of them become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations in the millimolar range in vivo, proteins are shown to change conformation from the prion
to non-prion state. This change requires a switch from a beta-sheet based structure to a alpha-helix based structure.
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 halide
s and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin
and few other proteins as a function of salt concentration.
Hydrochloride
In chemistry, hydrochlorides are salts resulting, or regarded as resulting, from the reaction of hydrochloric acid with an organic base . This is also known as muriate, derived from hydrochloric acid's other name: muriatic acid....
salt of guanidine
Guanidine
Guanidine is a crystalline compound of strong alkalinity formed by the oxidation of guanine. It is used in the manufacture of plastics and explosives. It is found in urine as a normal product of protein metabolism. The molecule was first synthesized in 1861 by the oxidative degradation of an...
.
Use in protein denaturation
Guanidinium chloride is one of the strongest denaturantDenaturation (biochemistry)
Denaturation is a process in which proteins or nucleic acids lose their tertiary structure and secondary structure by application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent , or heat...
s used in physiochemical studies of protein folding
Protein folding
Protein folding is the process by which a protein structure assumes its functional shape or conformation. It is the physical process by which a polypeptide folds into its characteristic and functional three-dimensional structure from random coil....
. In 6 molar guanidinium chloride solution, all protein
Protein
Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. A polypeptide is a single linear polymer chain of amino acids bonded together by peptide bonds between the carboxyl and amino groups of...
s with well ordered structure lose it, and most of them become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations in the millimolar range in vivo, proteins are shown to change conformation from the prion
Prion
A prion is an infectious agent composed of protein in a misfolded form. This is in contrast to all other known infectious agents which must contain nucleic acids . The word prion, coined in 1982 by Stanley B. Prusiner, is a portmanteau derived from the words protein and infection...
to non-prion state. This change requires a switch from a beta-sheet based structure to a alpha-helix based structure.
Historical survey
Petrunkin and Petrunkin (1927, 1928) appear to be the first who studied the binding of GndCl to gelatinGelatin
Gelatin is a translucent, colorless, brittle , flavorless solid substance, derived from the collagen inside animals' skin and bones. It is commonly used as a gelling agent in food, pharmaceuticals, photography, and cosmetic manufacturing. Substances containing gelatin or functioning in a similar...
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 halide
Halide
A halide is a binary compound, of which one part is a halogen atom and the other part is an element or radical that is less electronegative than the halogen, to make a fluoride, chloride, bromide, iodide, or astatide compound. Many salts are halides...
s and thiocyanates in following the liberation of sulfhydryl groups in ovalbumin
Ovalbumin
Ovalbumin is the main protein found in egg white, making up 60-65% of the total protein. Ovalbumin displays sequence and three-dimensional homology to the serpin superfamily, but unlike most serpins it is not a serine protease inhibitor...
and few other proteins as a function of salt concentration.