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- W1694821789 abstract "The acid-induced isomerization (the N-F transition) and expansion of sodium dodecyl sulfate-bovine plasma albumin complex (ADm;m, molar ratio of added sodium dodecyl sulfate to bovine plasma albumin; 0 ± m ± 12) were studied by measuring CD-resolved secondary structure, fluorescence polarization and lifetime of tryptophyl fluorophors, acid-titration with the electrostatic correction for the surface potential, 1H-n.m.r. spectra and cross relaxation time between irradiated and observed protons. The immobilization of tryptophyl fluorophors observed in the F-form of AD0 was suppressed in the F-form of AD10. The acid-titration analysis of AD12 showed non salt-bonding between carboxylate groups and cationic side chains in the F-form, as in the case of AD0, indicating charged side chains being presumably mobile. 1H-n.m.r. spectra and cross relaxation times between irradiated and observed protons in the F-form of AD10 indicated the increase in the local motion. On the other hand, AD10 and AD12 did not show any significant change in the CD-resolved secondary structure in the N-F transition region. The F-form of AD10 or AD12 may therefore be the molten-globule state which has secondary structure similar to the N-form of the complexes with fluctuating tertiary structure (side chains)." @default.
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- W1694821789 date "2009-01-12" @default.
- W1694821789 modified "2023-10-15" @default.
- W1694821789 title "Sodium dodecyl sulfate-bovine plasma albumin complex" @default.
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- W1694821789 doi "https://doi.org/10.1111/j.1399-3011.1985.tb03174.x" @default.
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