Cation-induced toroidal condensation of DNA studies with Co3+(NH3)6 |
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Authors: | J Widom R L Baldwin |
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Institution: | Medical Research Council Laboratory of Molecular Biology Hills Road Cambridge CB2 2QH, England;Department of Biochemistry University of Newcastle upon Tyne Newcastle upon Tyne NE1 7RU, England |
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Abstract: | The unfolding and refolding of Staphylococcus aureus penicillinase have been followed by urea-gradient electrophoresis. Unfolding of the native state proceeds by an all-or-none transition to fully unfolded protein, with no detectable accumulation of partially unfolded states. In contrast, refolding is complex and proceeds by very rapid, reversible formation of a partially folded state, H, which had been detected and characterized previously, as it is the most stable conformation at intermediate denaturant concentrations. At very low urea concentrations, a more compact conformational state was observed as a transient intermediate in refolding. There was little kinetic heterogeneity of the unfolded protein, as is normally observed with proteins containing proline residues. |
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