An electrophoretic study of reversible protein denaturation: chymotrypsinogen at high pressures.
When reversible denaturation of chymotrypsinogen is produced at elevated hydrostatic pressures, conformational relaxation can occur quite slowly, allowing electrophoretic separation of the principal states from the equilibrium mixture. In this work we report experimental concentration distribution patterns obtained at pH 2.03 at a temperature of 20.5 degrees and find them to be reasonably consistent with the behavior that is expected from a simple two-state isomerism. However, the results do not at all rule out the existence of low levels of intermediate states.
D002919:Chymotrypsinogen; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D013056:Spectrophotometry, Ultraviolet; D013696:Temperature; D013997:Time Factors
D002919:Chymotrypsinogen