Title : On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions.

Pub. Date : 2000 Jan 10

PMID : 10631479






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1 On the stabilizing action of protein denaturants: acetonitrile effect on stability of lysozyme in aqueous solutions. acetonitrile lysozyme Homo sapiens
2 Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change. acetonitrile lysozyme Homo sapiens
3 Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change. acetonitrile lysozyme Homo sapiens
4 At the higher MeCN content this dependence decreases until, at 0.06 mole fractions of MeCN, the difference in the preferential solvation between native and denatured lysozyme becomes independent of the temperature over a range of 60 K. The importance of taking into account non-ideality of a mixed solution, when analyzing preferential solvation phenomena was emphasized. acetonitrile lysozyme Homo sapiens
5 At the higher MeCN content this dependence decreases until, at 0.06 mole fractions of MeCN, the difference in the preferential solvation between native and denatured lysozyme becomes independent of the temperature over a range of 60 K. The importance of taking into account non-ideality of a mixed solution, when analyzing preferential solvation phenomena was emphasized. acetonitrile lysozyme Homo sapiens