title: The denatured states of ribonuclease-A: mechanism of denaturation by lithium chloride.
abstract: Denaturation of ribonuclease-A by lithium chloride has been studied using difference spectral, circular dichroic and viscometric measurements. The difference spectral results were interpreted in the light of our observations that the solvent effect of the denaturant on the tyrosyl residue is non-linear. It has been observed that (1) the lithium chloride-denatured protein contains 3% alpha-helix and 18% beta-structure, and (2) only two of the three buried tyrosyl residues are normalized in the denatured protein.
authors.forename: F
authors.initials: F
authors.lastname: Ahmad
authors.forename: L A
authors.initials: LA
authors.lastname: Khan
mesh_terms: D002712:Chlorides / Q000494:pharmacology*; D002942:Circular Dichroism; D008094:Lithium / Q000494:pharmacology*; D018021:Lithium Chloride; D011489:Protein Denaturation / Q000187:drug effects; D012259:Ribonuclease, Pancreatic; D013057:Spectrum Analysis; D014783:Viscosity
chemical_list: D002712:Chlorides; D008094:Lithium; D012259:Ribonuclease, Pancreatic; D018021:Lithium Chloride