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Further Evidence on the Equilibrium “Pre-molten Globule State”: Four-state Guanidinium Chloride-induced Unfolding of Carbonic Anhydrase B at Low Temperatureстатья
- Авторы: Uversky Vladimir N., Ptitsyn Oleg B.
- Журнал: Journal of Molecular Biology
- Том: 255
- Номер: 1
- Год издания: 1996
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 215
- Последняя страница: 228
- DOI: 10.1006/jmbi.1996.0018
- Аннотация: 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 beta-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.
- Добавил в систему: Уверский Владимир Николаевич