Increasing charge while preserving noncovalent protein complexes for ESI-MS
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چکیده
منابع مشابه
Positive and negative ion mode ESI-MS and MS/MS for studying drug-DNA complexes
We report systematic investigation of duplex DNA complexes with minor groove binders (Hoechst 33258, Hoechst 33342, Netropsin and DAPI) and intercalators (daunomycin, doxorubicin, actinomycin D, ethidium, cryptolepine, neocryptolepine, m-Amsacrine, proflavine, ellipticine and mitoxantrone) by ESI-MS and ESI-MS/MS in the negative ion mode and in the positive ion mode. The apparent solution phase...
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Electrospray time-of-flight mass spectrometry was used to quantitatively determine the dissociation constant of chorismate mutase and a transition state analogue inhibitor. This system presents a fairly complex stoichiometry because the native protein is a homotrimer with three equal and independent substrate binding sites. We can detect the chorismate mutase trimer as well as chorismate mutase...
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Studying noncovalent protein complexes by electrospray ionization mass spectrometry.
Electrospray ionization mass spectrometry has been used to study protein interactions driven by noncovalent forces. The gentleness of the electrospray ionization process allows intact protein complexes to be directly detected by mass spectrometry. Evidence from the growing body of literature suggests that the ESI-MS observations for these weakly bound systems reflect, to some extent, the nature...
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ژورنال
عنوان ژورنال: Journal of the American Society for Mass Spectrometry
سال: 2009
ISSN: 1044-0305,1879-1123
DOI: 10.1016/j.jasms.2008.11.013