Extensive unfolding of the C-LytA choline-binding module by submicellar concentrations of sodium dodecyl sulphate
We have investigated the stability of the choline-binding module C-LytA against sodium dodecyl sulphate (SDS)-induced unfolding at pH 7.0 and 20 C. A major intermediate with an unfolded N-terminal region accumulates at around 0.75 mM SDS, whereas 2.0 mM SDS was sufficient for a complete unfolding. T...
| Autores: | , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2006 |
| País: | España |
| Institución: | Universidad Miguel Hernández de Elche |
| Repositorio: | REDIUMH. Depósito Digital de la UMH |
| OAI Identifier: | oai:dspace.umh.es:11000/30953 |
| Acceso en línea: | https://hdl.handle.net/11000/30953 |
| Access Level: | acceso abierto |
| Palabra clave: | Choline-binding module SDS denaturation Protein stability Repeat proteins Affinity tag |
| Sumario: | We have investigated the stability of the choline-binding module C-LytA against sodium dodecyl sulphate (SDS)-induced unfolding at pH 7.0 and 20 C. A major intermediate with an unfolded N-terminal region accumulates at around 0.75 mM SDS, whereas 2.0 mM SDS was sufficient for a complete unfolding. This might be the first report of a protein being extensively unfolded by submicellar concentrations of SDS, occurring through formation of detergent clusters on the protein surface. All transitions were reversible upon SDS complexation with b-cyclodextrin, allowing the calculation of thermodynamic parameters. A model for the unfolding of C-LytA by SDS is presented and compared to a previous denaturation scheme by guanidine hydrochloride. |
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