Circumnavigating misfolding traps in the energy landscape through protein engineering: suppression of molten globule and aggregation in carbonic anhydrase

The native state of the enzyme human carbonic anhydrase is stabilized by the introduction of a disulfide bond, the oxidized A23C/L203C mutant. Improved refolding yields are possible to achieve, if the immergence of aggregation-prone intermediates such as the molten globule can be controlled.