<p>Mass spectrometry-based gas-phase ion/ion reactions have
grown considerably in the last decade. Their applications range from structural
elucidation, instrument calibration, and spectral deconvolution. One field that
has been amenable to these methods is proteomic studies. Proteins and peptides
have grown as candidates for biomarkers and vaccines. Proteins are vastly
different with mass ranging from 1 kDa to well over 1 MDa and various types of
post translational modifications. The structural heterogeneity that proteins
can exhibit demonstrates the need for high resolution mass spectrometry
methods. The combination of native mass
spectrometry and soft ionization sources allow for preservation of structures
seen in solution as analytes enter the gas phase. By developing methods that
probe these structures, the information gathered can be related to the native
structures in solution. Here I show, gas
phase ion/ion reactions that can be utilized for location of salt bridge
structures, gas-phase crosslinking of homo and heterodimer protein complexes,
and mass determination of large (>800 kDa) protein complexes. These methods
allow for greater control, faster data acquisition, and minimal sample
preparation. These methods were developed on modified Sciex TripleTOF 5600 and
4000 QTRAP tandem mass spectrometers.</p>
| Identifer | oai:union.ndltd.org:purdue.edu/oai:figshare.com:article/14843505 |
| Date | 23 July 2021 |
| Creators | Anthony Marcel Pitts-Mccoy (11024205) |
| Source Sets | Purdue University |
| Detected Language | English |
| Type | Text, Thesis |
| Rights | CC BY 4.0 |
| Relation | https://figshare.com/articles/thesis/DEVELOPMENT_OF_GAS-PHASE_ION_ION_REACTIONS_FOR_CHARACTERIZING_PROTEIN_AND_PEPTIDE_IONS/14843505 |
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