ArticleJournal of the American Society for Mass Spectrometry2009
The use of ECD/ETD to identify the site of electrostatic interaction in noncovalent complexes.
Article in Journal of the American Society for Mass Spectrometry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed.
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- Effective discrimination of gas-phase peptide conformers using TIMS-ECD-ToF MS/MS.Analytical methods : advancing methods and applications · 2021Article
- Higher-order structural characterisation of native proteins and complexes by top-down mass spectrometry.Chemical science · 2020Review
- Structural Analysis of 14-3-3-ζ-Derived Phosphopeptides Using Electron Capture Dissociation Mass Spectrometry, Traveling Wave Ion Mobility Spectrometry, and Molecular Modeling.The journal of physical chemistry. B · 2020Article
- Top or Middle? Up or Down? Toward a Standard Lexicon for Protein Top-Down and Allied Mass Spectrometry Approaches.Journal of the American Society for Mass Spectrometry · 2019Article
- Phosphopeptide Fragmentation and Site Localization by Mass Spectrometry: An Update.Analytical chemistry · 2019Review
- Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Mass spectrometry reviews · 2018Review
- Influence of Sulfolane on ESI-MS Measurements of Protein-Ligand Affinities.Journal of the American Society for Mass Spectrometry · 2016Article
- The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes.Protein science : a publication of the Protein Society · 2015Review
- Probing the electron capture dissociation mass spectrometry of phosphopeptides with traveling wave ion mobility spectrometry and molecular dynamics simulations.Journal of the American Society for Mass Spectrometry · 2015Article
- A peptide targeting an interaction interface disrupts the dopamine D1-D2 receptor heteromer to block signaling and function in vitro and in vivo: effective selective antagonism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- MALDI/post ionization-ion mobility mass spectrometry of noncovalent complexes of dopamine receptors' epitopes.Journal of proteome research · 2013Article
- Integrating Native Mass Spectrometry and Top-Down MS for Defining Protein Interactions Important in Biology and Medicine.Mass spectrometry (Tokyo, Japan) · 2013Article
- Covalent and non-covalent binding in the ion/ion charge inversion of peptide cations with benzene-disulfonic acid anions.Journal of mass spectrometry : JMS · 2012Article
- Higher-order structure of nucleic acids in the gas phase: top-down analysis of base-pairing interactions.International journal of mass spectrometry · 2012Article
- Elucidating the site of protein-ATP binding by top-down mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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.
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Registered trials
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