Abstract
The higher order protein structure was investigated by chemical oxidation and high resolution mass spectrometry. Ascorbate and the iron-EDTA solutions were added in a 1:10 dilution to 200 μM apomyoglobin in 50 mM sodium phosphate (pH 6.5). To analyze the extent to apomyoglobin oxidation, the oxidized apomyoglobin was purified using a C4 ZipTip, and the protein was eluted into a total of 60-80 μL of acetonitrile with 0.1% trifluoroacetic acid. Analysis of the oxidation products by ES-FT-ICR-MS showed that oxidation of apomyoglobin occurs in a time-dependent manner, and a large number of amino acid side chain oxygenation events can be detected before significant backbone cleavage occurs.
| Original language | English |
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| Pages | 329-330 |
| Number of pages | 2 |
| State | Published - 2002 |
| Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Conference
| Conference | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
|---|---|
| Country/Territory | United States |
| City | Orlando, FL |
| Period | 06/2/02 → 06/6/02 |