Protein conformational changes and myelin solubilization by anion-detergent solutions.
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.
Monreal
J
J
Institute Cajal, CSIC, Madrid, Spain.
Carmona
P
P
Regueiro
P
P
Díaz
R S
RS
D000818:Animals; D002417:Cattle; D003902:Detergents; D009185:Myelin Proteins / Q000737:chemistry*; D011487:Protein Conformation; D012995:Solubility; D012996:Solutions; D013055:Spectrophotometry, Infrared
D003902:Detergents; D009185:Myelin Proteins; D012996:Solutions