The use of ECD/ETD to identify the site of electrostatic interaction in noncovalent complexes View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2009-02

AUTHORS

Shelley N. Jackson, Sucharita Dutta, Amina S. Woods

ABSTRACT

Electrostatic interactions play an important role in the formation of noncovalent complexes. Our previous work has highlighted the role of certain amino acid residues, such as arginine, glutamate, aspartate, and phosphorylated/sulfated residues, in the formation of salt bridges resulting in noncovalent complexes between peptides. Tandem mass spectrometry (MS) studies of these complexes using collision-induced dissociation (CID) have provided information on their relative stability. However, product-ion spectra produced by CID have been unable to assign specifically the site of interaction for the complex. In this work, tandem MS experiments were conducted on noncovalent complexes using both electron capture dissociation (ECD) and electron-transfer dissociation (ETD). The resulting spectra were dominated by intramolecular fragments of the complex with the electrostatic interaction site intact. Based upon these data, we were able to assign the binding site for the peptides forming the noncovalent complex. More... »

PAGES

176-179

References to SciGraph publications

  • 2001-01. A Study of peptide-peptide interaction by matrix-assisted laser desorption/ionization in JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
  • 2008-06. Electron capture/transfer versus collisionally activated/induced dissociations: Solo or duet? in JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
  • 2005-06. Role of electrostatic interaction in receptor-receptor heteromerization in JOURNAL OF MOLECULAR NEUROSCIENCE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1016/j.jasms.2008.08.021

    DOI

    http://dx.doi.org/10.1016/j.jasms.2008.08.021

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1001558792

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/18835725


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