Abstract
The disulfide structure of a 6-cystine-containing protein was discussed. The negative signature mass (NSM) algorithm was used to interpret mass spectral data. It was used to eliminate possible disulfide linkages based on mass spectrometric data. The logic assumed complete cyanylation of all free thiols following partial reduction. The disulfide structure of the 12-cysteine containing Transforming Growth Factor-β Type II Receptor was determined through the chemical techniques of partial reduction, thiol cyanylation, protein backbone cleavage and mass mapping using the NSM algorithm for data processing.
Original language | English (US) |
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Title of host publication | Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics |
Pages | 335-336 |
Number of pages | 2 |
State | Published - 2002 |
Externally published | Yes |
Event | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002 |
Other
Other | Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics |
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Country/Territory | United States |
City | Orlando, FL |
Period | 6/2/02 → 6/6/02 |
ASJC Scopus subject areas
- Spectroscopy