‘All-or-none’ mechanism of the molten globule unfolding
Autor: | Roger H. Pain, Oleg B. Ptitsyn, Gennady V. Semisotnov, Vladimir N. Uversky |
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Rok vydání: | 1992 |
Předmět: |
Protein Denaturation
Carbonic anhydrase B Circular dichroism Biophysics Guanidines Biochemistry beta-Lactamases Carbonic Anhydrase B Size exclusion chromatography Structural Biology Genetics Native state Denaturation (biochemistry) Protein folding Molecular Biology Guanidine β-Lactamase Carbonic Anhydrases Chromatography Dose-Response Relationship Drug Molecular dimensions Chemistry Fast protein liquid chromatography Cell Biology Molten globule Cold Temperature Crystallography Models Chemical Chromatography Gel |
Zdroj: | FEBS Letters. 314:89-92 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(92)81468-2 |
Popis: | The Gdm-HCl-induced unfolding of bovine carbonic anhydrase B and S. aureus beta-lactamase was studied at 4 degrees C by a variety of methods. With the use of FPLC it has been shown that within the transition from the molten globule to the unfolded state the distribution function of molecular dimensions is bimodal. This means that equilibrium intermediates between the molten globule and the unfolded states are absent, i.e. the molten globule unfolding follows the 'all-or-none' mechanism. |
Databáze: | OpenAIRE |
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