The design and incorporation of a decelerating/accelerating cell into a reflectron
time-of-flight mass spectrometer is described for the examination of promptly-formed
photodissociation products of peptide ions. The analytical utility of prompt 193-nm
photodissociation was investigated for model peptides that resemble tryptic digest
products, as well as for two sets of homologous peptides. The first of these sets include
bradykinin, several bradykinin fragments, and two bradykinin mutants with substituted
amino acids. Fragment ion spectra of [M + H]+, [M + Na]+, and [M + Cu]+ were
collected for each of these peptides. The second set of homologous peptides has the
sequence XVGVAZG, where variable amino acid X was either arginine, histidine, or
lysine, and amino acid Z was either proline, serine, or glycine. Photofragment ion
spectra obtained using the new mass spectrometer are compared to results of high energy
collision induced dissociation (CID) acquired on a high performance commercial
instrument. The advantages and disadvantages of prompt photodissociation relative to
CID are discussed, as well as the advantages of photodissociation using the modified
instrument geometry versus that of the post-source decay focusing method.
| Identifer | oai:union.ndltd.org:tamu.edu/oai:repository.tamu.edu:1969.1/3293 |
| Date | 12 April 2006 |
| Creators | Morgan, Joseph William |
| Contributors | Russell, David H. |
| Publisher | Texas A&M University |
| Source Sets | Texas A and M University |
| Language | en_US |
| Detected Language | English |
| Type | Book, Thesis, Electronic Dissertation, text |
| Format | 23244524 bytes, electronic, application/pdf, born digital |
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