
AbstractWell‐resolved ion signals of intact large protein assemblies, with molecular masses extending above one million Dalton, have been detected and mass analyzed using electrospray ionization mass spectrometry, with an uncertainty in mass of <0.2%. the mass spectral data seem to reflect known solution‐phase behavior of the studied protein assembly and have therefore been directly used to probe the protein assembly topology and stability as a function of ionic strength and ph.
Models, Molecular, Noncovalent interactions, Osmolar Concentration, Farmacie(FARM), Hydrogen-Ion Concentration, Mass Spectrometry, Molecular Weight, Alcohol Oxidoreductases, Electrospray ionization mass spectrometry, Protein assemblies, Protein Structure, Quaternary, Vanillyl-alcohol oxidase
Models, Molecular, Noncovalent interactions, Osmolar Concentration, Farmacie(FARM), Hydrogen-Ion Concentration, Mass Spectrometry, Molecular Weight, Alcohol Oxidoreductases, Electrospray ionization mass spectrometry, Protein assemblies, Protein Structure, Quaternary, Vanillyl-alcohol oxidase
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