Guanidinium chloride

Guanidinium chloride

Names
IUPAC name Carbamimidoylazanium chloride
Other names Guanidine hydrochloride
Identifiers
CAS Number	50-01-1 Y
3D model (Jmol)	Interactive image
ChEBI	CHEBI:32735 Y
ChemSpider	5540 Y
ECHA InfoCard	100.000.003
PubChem CID	10855382
UNII	3YQC9ZY4YB Y
InChI InChI=1S/CH5N3.ClH/c2-1(3)4;/h(H5,2,3,4);1H Y Key: PJJJBBJSCAKJQF-UHFFFAOYSA-N Y InChI=1/CH5N3.ClH/c2-1(3)4;/h(H5,2,3,4);1H Key: PJJJBBJSCAKJQF-UHFFFAOYAG
SMILES Cl.[N@H]=C(N)N
Properties
Chemical formula	CH6ClN3
Molar mass	95.53 g·mol−1
Appearance	orthorhombic bipyramidal crystals
Density	1.354 g/cm3 at 20 °C
Melting point	182.3 °C (360.1 °F; 455.4 K)
Solubility in water	very soluble in water and ethanol
Hazards
Safety data sheet	External MSDS
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Y  (what is YN ?)
Infobox references

Guanidinium chloride or guanidine hydrochloride, usually abbreviated GuHCl and sometimes GdnHCl or GdmCl, is the hydrochloride salt of guanidine.

Guanidinium chloride crystallizes in orthorhombic space group Pbca. The crystal structure consists of a network of guanidinium cations and chloride anions linked by N–H···Cl hydrogen bonds.

Guanidinium chloride is a strong chaotrope and one of the strongest denaturants used in physiochemical studies of protein folding. At high concentrations of guanidinium chloride (e.g., 6 M), proteins lose their ordered structure, and they tend to become randomly coiled, i.e. they do not contain any residual structure. However, at concentrations in the millimolar range in vivo, guanidinium chloride has been shown to "cure" prion positive cells (i.e. cells exhibiting a prion positive phenotype revert to a prion negative phenotype). This is the result of inhibition of the Hsp104 chaperone protein known to play an important role in prion fiber fragmentation and propagation.

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 thiocyanates in following the liberation of sulfhydryl groups in ovalbumin and few other proteins as a function of salt concentration.