Literature DB >> 10948502

Multiple and subsequent MALDI-MS on-target chemical reactions for the characterization of disulfide bonds and primary structures of proteins.

H P Happersberger1, M Bantscheff, S Barbirz, M O Glocker.   

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Year:  2000        PMID： 10948502     DOI： 10.1385/1-59259-045-4:167

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


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  3 in total

1.  Possible evidence of amide bond formation between sinapinic acid and lysine-containing bacterial proteins by matrix-assisted laser desorption/ionization (MALDI) at 355 nm.

Authors:  Clifton K Fagerquist; Omar Sultan; Michelle Q Carter
Journal:  J Am Soc Mass Spectrom       Date:  2012-10-02       Impact factor: 3.109

2.  Covalent attachment and dissociative loss of sinapinic acid to/from cysteine-containing proteins from bacterial cell lysates analyzed by MALDI-TOF-TOF mass spectrometry.

Authors:  Clifton K Fagerquist; Brandon R Garbus; Katherine E Williams; Anna H Bates; Leslie A Harden
Journal:  J Am Soc Mass Spectrom       Date:  2010-01-25       Impact factor: 3.109

3.  A new method for analysis of disulfide-containing proteins by matrix-assisted laser desorption ionization (MALDI) mass spectrometry.

Authors:  Hongmei Yang; Ning Liu; Xiaoyan Qiu; Shuying Liu
Journal:  J Am Soc Mass Spectrom       Date:  2009-09-03       Impact factor: 3.109
  3 in total

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