GuHC1 induced unfolding-folding transition of a hinge-bending protein: horse muscle phosphoglycerate kinase.
The unfolding-folding transition of phosphoglycerate kinase induced by GuHC1 was studied at equilibrium. Various signals were used to follow the transition: fluorescence emission, difference spectra, circular dichroism and enzymatic activity. The non-coincidence of transition curves obtained from different structural parameters indicate a deviation from a two-state process. The view that structural domains behave as independent "folding units" is critically discussed.
D000818:Animals; D002942:Circular Dichroism; D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology*; D006736:Horses; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D010735:Phosphoglycerate Kinase / Q000378:metabolism*; D011487:Protein Conformation; D011489:Protein Denaturation; D013050:Spectrometry, Fluorescence
D006146:Guanidines; D010735:Phosphoglycerate Kinase; D019791:Guanidine