Spectroscopic Studies of Ferrocytochrome c Folding

Abstract

Electron-transfer triggering has been employed in a comparison of the folding energetics and kinetics of cytochrome c from horse and Saccharomyces cerevisiae. These two proteins, with just 60% sequence identity but very similar backbone structures, fold at very different rates at a given denaturant concentration, but at nearly the same rate when their folding free energies are the same. Differences in the amino-acid sequences shift the position of the folding/unfolding equilibrium, but do not appear to alter the location of the transition state along the folding coordinate.

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