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Extensive unfolding of the C‐LytA choline‐binding module by submicellar concentrations of sodium dodecyl sulphate
Author(s) -
Maestro Beatriz,
Sanz Jesús M.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.042
Subject(s) - chemistry , guanidine , sodium dodecyl sulfate , denaturation (fissile materials) , sodium , chromatography , hydrochloride , crystallography , nuclear chemistry , biochemistry , organic chemistry
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 β‐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.