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A) Reaction coordinate diagram. (B) The equilibrium unfolding transition. (C) Relaxation time as a function of the final dénaturant concentration. 0 C Dénaturant] ix\r [Dénaturant] FIGURE 3-5 Equilibrium and kinetic characteristics of wild-type (—) and kinetic mutant (—). (A) Reaction coordinate diagram. (B) The equilibrium unfolding tran sition. (C) Relaxation time as a function of the final dénaturant concentration. relaxation times for refolding are equivalent to the values of the parent protein (see Figure 3-4C); however, the relaxation times for unfolding are increased.
Coli and can be purified for our studies. Mutations which greatly destabilize the protein and presumably lead to proteolysis or aggregation could conceivably alter the pathway of folding. The ability to interpret the data from the study of mutant proteins in terms of a structural model depends in part upon the ability to recognize patterns within the data. The recognition of patterns in turn depends upon the ability to categorize the data in a simple, yet informative, manner. We have previously developed a scheme for categorizing equilibrium and kinetic folding data which allows us to analyze variant proteins (Beasty et al.
2 Experimental Strategies 43 Unfolding at a Single Final Dénaturant Concentration TIME B ui 2 < X < LÜ or o o Refolding Unfolding [DENATURANT] FIGURE 3-2 Kinetic study of protein folding. (A) The transient exponential re sponse of protein unfolding in a given final concentration of dénaturant. (B) Expected dependence of the logarithm of the relaxation time on the final dénaturant concen tration for a two-state folding reaction. , high dénaturant concentration). Within the transition zone, the logarithm of r reaches a maximum, and, for a reversible process, the log rs obtained from refolding and unfolding experiments meet smoothly.