Effects of urea and trimethylamine-N-oxide (TMAO) on the interactions of lysozyme in solution.
The effect of two physiological cosolutes (urea and trimethylamine-N-oxide) and of KCl on the intermolecular interactions in concentrated lysozyme solutions were studied by synchrotron radiation small angle x-ray scattering. The evolution of the structure factors as a function of cosolute and/or salt concentration was modeled using pair potentials following an approach recently described in the literature. It was found that the structure factors for salt and/or cosolute concentration series at a fixed protein concentration can best be described using a variable depth attractive potential and a constant effective charge rather than a constant attractive potential and a variable effective charge as done in previous work.
European Molecular Biology Laboratory, Hamburg Outstation, D-22603 Hamburg, Germany.
Marc
M
Niebuhr
Michel H J
MH
Koch
D000818:Animals; D001703:Biophysics / Q000379:methods*; D004305:Dose-Response Relationship, Drug; D006863:Hydrogen-Ion Concentration; D008744:Methylamines / Q000737:chemistry*; D015233:Models, Statistical; D046912:Multiprotein Complexes / Q000737:chemistry; D009113:Muramidase / Q000737:chemistry*; D011189:Potassium Chloride / Q000737:chemistry*; D011489:Protein Denaturation; D012542:Scattering, Radiation; D012996:Solutions; D017356:Synchrotrons; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors; D014508:Urea / Q000737:chemistry*; D014867:Water / Q000737:chemistry; D014965:X-Rays
D008744:Methylamines; D046912:Multiprotein Complexes; D012996:Solutions; D014867:Water; D011189:Potassium Chloride; D014508:Urea; D009113:Muramidase; C005855:trimethyloxamine