Abstract
Heats of solution for myelin basic protein have been determined using microcalorimetry. All aqueous systems studies yielded negative heats of solution; in contrast, trifluoroethanol produced a small positive heat of solution, while reaction with dimethyl sulfoxide was strikingly exothermic. The heat of interaction for native myelin basic protein with 8 M urea at pH 4.0, 29°C, was found to be −79 ± 16 kcal/mol. The significance of these results in terms of the protein's structural organization is discussed.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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