Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping--a novel approach to assess intermolecular protein contacts.

@article{Bennett2000ChemicalCW,
  title={Chemical cross-linking with thiol-cleavable reagents combined with differential mass spectrometric peptide mapping--a novel approach to assess intermolecular protein contacts.},
  author={Keiryn Lynn Bennett and M Kussmann and Per Bjoerk and M Godzwon and Mette Hjorth Mikkelsen and Palle Gravgaard S{\o}rensen and Peter Roepstorff},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 8},
  pages={
          1503-18
        }
}
The intermolecular contact regions between monomers of the homodimeric DNA binding protein ParR and the interaction between the glycoproteins CD28 and CD80 were investigated using a strategy that combined chemical cross-linking with differential MALDI-MS analyses. ParR dimers were modified in vitro with the thiol-cleavable cross-linker 3,3'-dithio-bis(succinimidylproprionate) (DTSSP), proteolytically digested with trypsin and analyzed by MALDI-MS peptide mapping. Comparison of the peptide maps… CONTINUE READING
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