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Protein conformational changes and myelin solubilization by anion‐detergent solutions
Author(s) -
Monreal Jaime,
Carmona Pedro,
Regueiro Pilar,
Diaz Ricardo S.
Publication year - 1992
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 - 10.1016/0014-5793(92)80810-4
Subject(s) - chemistry , solubility , myelin , phosphate , solubilization , sodium , sodium dodecyl sulfate , denaturation (fissile materials) , conformational change , sulfate , amide , chromatography , myelin basic protein , biophysics , biochemistry , nuclear chemistry , organic chemistry , neuroscience , biology , central nervous system
The addition of sodium sulfate to a myelin suspension in sodium phosphate buffer at neutral pH, containing octyl glucoside detergent (OG), increases the membrane solubility more than 5‐fold by an unknown structural mechanism. FTIR spectroscopy has been applied to investigate anion effects on the conformational structure of myelin proteins. Sulfate and sulfate‐phosphate media, but not phosphate alone, induce a great conformational protein disorder. The addition of the detergent to the anion mixture solution prevents the myelin from protein denaturation. The conformational transitions have also been quantified through the amide I region. Explanations of these changes and their connections with myelin solubility are also included.