Signature Sets', Minimal Fragment Sets for Identifying Protein Disulfide Structures with Cyanylation-Based Mass Mapping Methodology

Our cyanylation (CN)-based methodology for determining disulfide structure of cystinyl proteins overcomes the limitations of conventional proteolytic methods. However, the CN-based method has the potential drawback that occasionally some CN-induced cleavage fragments may not be detected. We show tha...

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Bibliographic Details
Published inJournal of proteome research Vol. 3; no. 4; pp. 770 - 777
Main Authors Wu, Wei, Huang, Wei, Qi, Jianfeng, Chou, Yi-Te, Torng, Eric, Watson, J. Throck
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 01.07.2004
Subjects
Cyanides - chemistry
Cystine - analysis
Cystine - chemistry
Disulfides - chemistry
Oxidation-Reduction
Peptide Fragments - chemistry
Peptide Mapping - methods
Peptides - chemistry
Protein Structure, Tertiary
Proteins - chemistry
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Summary:Our cyanylation (CN)-based methodology for determining disulfide structure of cystinyl proteins overcomes the limitations of conventional proteolytic methods. However, the CN-based method has the potential drawback that occasionally some CN-induced cleavage fragments may not be detected. We show that CN-based methods can overcome the failure to detect fragments by demonstrating the existence of small ‘signature sets' of fragments. The link between signature sets and the robustness of CN-based methodology is validated by two case studies. Keywords: disulfide structure • cystinyl protein • signature sets • disulfide mass mapping
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ISSN:1535-3893
1535-3907
DOI:10.1021/pr049961t