Surfactant effects on protein structure examined by electrospray ionization mass spectrometry
نویسندگان
چکیده
منابع مشابه
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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The structure of melittin in the presence of dioleoylphosphatidylcholine (DOPC) was investigated using hydrogen deuterium (H/D) exchange in conjunction with collision induced dissociation (CID) in an rf-only hexapole ion guide with electrospray ionization-Fourier transform ion cyclotron resonance mass spectrometry (ESI-FT-ICR MS). The deuterium incorporation into backbone amide hydrogens of mel...
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BACKGROUND Matrix effects can profoundly reduce the performance of electrospray ionization mass spectrometry. Preliminary observations indicated that the methanol used in the mobile phase could be a source of differential ionization or ion suppression. METHODS Drug stability studies, analysis of biological extracts, mixing experiments, and postcolumn infusions were used to test 9 commercial m...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1994
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560031109