Fig. 5
From: Complex kinetics and residual structure in the thermal unfolding of yeast triosephosphate isomerase
Fractional structural change for the two kinetic steps in Scheme 2 at different temperatures. Fractional changes in ellipticity were calculated from eqns. 2 and 3 from values of the rate constants and amplitudes determined at pH 6.7. Data for step I → X, i.e., (θX−θI)/(θU−θI), are shown as circles; data for step X → U, i.e., (θU−θX)/(θU−θI), are shown as squares