Further Evidence on the Equilibrium “Pre-molten Globule State”: Four-state Guanidinium Chloride-induced Unfolding of Carbonic Anhydrase B at Low Temperature
Protein Folding, Molten Globule, Carbonic Anhydrase, Size-exclusion Chromatography
Digital Object Identifier (DOI)
Equilibrium guanidinium chloride-induced unfolding of bovine carbonic anhydrase NB has been investigated by a combination of optical methods with size-exclusion chromatography. It has been shown that, as in the case of staphylococcal β-lactamase, bovine carbonic anhydrase B unfolds at low temperature through two equilibrium intermediates; the molten globule and the pre-molten globule states. This pre-molten globule state has a hydrodynamic volume no more than twofold larger than that of the native state, i.e. is relatively compact. It has a pronounced far UV CD spectrum, suggesting the presence of a substantial secondary structure. It binds 8-anilinonaphthalene-1-sulphonate (though weaker than the molten globule state), which suggests the formation of solvent-exposed clusters of non-polar groups. Thus, this novel state of protein molecules shares a number of properties with the “burst” kinetic intermediate of protein folding and can be considered as its equilibrium counterpart.
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Citation / Publisher Attribution
Journal of Molecular Biology, v. 255, issue 1, p. 215-228
Scholar Commons Citation
Uversky, Vladimir N. and Ptitsyn, Oleg B., "Further Evidence on the Equilibrium “Pre-molten Globule State”: Four-state Guanidinium Chloride-induced Unfolding of Carbonic Anhydrase B at Low Temperature" (1996). Molecular Medicine Faculty Publications. 635.