Further evidence on the equilibrium 'pre-molten globule state': four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature
| Autor: | Vladimir N. Uversky, Ptitsyn Ob |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Guanidinium chloride
Protein Denaturation Protein Folding Size-exclusion chromatography Guanidines Anilino Naphthalenesulfonates Protein Structure Secondary chemistry.chemical_compound Structural Biology Carbonic anhydrase Native state Animals Guanidine Molecular Biology Protein secondary structure Carbonic Anhydrases Fluorescent Dyes biology Chemistry Molten globule Cold Temperature Crystallography biology.protein Protein folding Cattle |
| Zdroj: | Journal of molecular biology. 255(1) |
| ISSN: | 0022-2836 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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