Determination of the disulfide structure of a 6-cystine-containing protein using a "negative signature mass" algorithm to interpret mass spectral data

Chad Borges, Jianfeng Qi, Wei Wu, J. Throck Watson

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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 languageEnglish (US)
Title of host publicationProceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages335-336
Number of pages2
StatePublished - 2002
Externally publishedYes
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

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ASJC Scopus subject areas

  • Spectroscopy

Cite this

Borges, C., Qi, J., Wu, W., & Watson, J. T. (2002). Determination of the disulfide structure of a 6-cystine-containing protein using a "negative signature mass" algorithm to interpret mass spectral data. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 335-336)