An investigation of the thermal unfolding of swine pepsinogen using circular dichroism.
The thermal unfolding of swine pepsinogen is investigated using circular dichroism (CD) in the pH range 6-9. CD spectra and single wavelength melting curves are analyzed to show the presence of two resolvable transitions. Analysis of difference CD spectra by the method of singular value decomposition indicates that the changes in conformation are distinct in the two transitions. Single wavelength melting curves show that only one of the transitions has a strong pH dependence. The results are discussed in terms of earlier kinetic and calorimetric data to suggest the presence of one or more intermediates in the reaction.
McPhie
P
P
Laboratory of Biochemistry and Metabolism, NIDDK, NIH, Bethesda, Maryland 20892.
Shrager
R I
RI
D000818:Animals; D002942:Circular Dichroism; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D010435:Pepsinogens / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D013552:Swine; D013816:Thermodynamics
D010435:Pepsinogens