Relative Dissociation Energies of Protonated Peptides by Electrospray Ionization/Surface-Induced Dissociation
β Scribed by Lim, Hanjo; Schultz, David G.; Yu, Chongwoo; Hanley, Luke
- Book ID
- 126183777
- Publisher
- American Chemical Society
- Year
- 1999
- Tongue
- English
- Weight
- 141 KB
- Volume
- 71
- Category
- Article
- ISSN
- 0003-2700
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We report here surface-induced dissociation spectra of three multiply charged peptides: doubly protonated angiotensin I, doubly protonated renin substrate, and triply protonated melittin. For comparison, the collision-activated dissociation spectra of renin substrate and melittin are also presented.
The grazing incidence surface-induced dissociation (GI-SID) of various protonated peptides with typical kinetic energies of 350 eV was investigated. Peptide ions were generated by matrix-assisted laser desorption/ ionization (MALDI) using delayed extraction. The collision target surfaces used were a
## Abstract The internal energy of ions and the timescale play fundamental roles in mass spectrometry. The main objective of this study is to estimate and compare the internal energy distributions of different ions (different nature, degree of freedom βDOFβ and fragmentations) produced in an electr