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New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra

Title
New algorithm for the identification of intact disulfide linkages based on fragmentation characteristics in tandem mass spectra
Authors
Choi S.Jeong J.Na S.Lee H.S.Kim H.-Y.Lee K.-J.Paek E.
Ewha Authors
이공주
SCOPUS Author ID
이공주scopus
Issue Date
2010
Journal Title
Journal of Proteome Research
ISSN
1535-3893JCR Link
Citation
vol. 9, no. 1, pp. 626 - 635
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Identifying the sites of disulfide bonds in a protein is essential for thorough understanding of a protein's tertiary and quaternary structures and its biological functions. Disulfide linked peptides are usually identified indirectly by labeling free sulfhydryl groups with alkylating agents, followed by chemical reduction and mass spectral comparison or by detecting the expected masses of disulfide linked peptides on mass scan level. However, these approaches for determination of disulfide bonds become ambiguous when the protein is highly bridged and modified. For accurate identification of disulfide linked peptides, we present here an algorithmic solution for the analysis of tandem mass (MS/MS) spectra of disulfide bonded peptides under nonreducing condition. A new algorithm called "DBond" analyzes disulfide linked peptides based on specific features of disulfide bonds. To determine disulfide linked sites, DBond takes into account fragmentation patterns of disulfide linked peptides in nucleoside diphosphate kinase (NDPK) as a model protein, considering fragment ions including cysteine, cysteine thioaldehyde (-2 Da, CT), cysteine persul-fide (+32 Da, CS) and dehydroalanine (-34 Da, CΔ). Using this algorithm, we successfully identified about a dozen novel disulfide bonds in a hexa EF-hand calcium binding protein secretagogin and in a methionine sulfoxide reductase. We believe that DBond, taking into account the disulfide bond fragmentation characteristics and post-translational modifications, offers a novel approach for automatic identification of unknown disulfide bonds and their sites in proteins from MS/MS spectra. © 2010 American Chemical Society.
DOI
10.1021/pr900771r
Appears in Collections:
약학대학 > 약학과 > Journal papers
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