ArticleProtein science : a publication of the Protein Society2015
Does deamidation cause protein unfolding? A top-down tandem mass spectrometry study.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Mechanism-Driven Features Enable Asn Deamidation Reactivity Prediction via Machine Learning Methods.Journal of chemical information and modeling · 2025Article
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- Heat-induced structural and chemical changes to a computationally designed miniprotein.Protein science : a publication of the Protein Society · 2024Article
- Wheat-Based Glues in Conservation and Cultural Heritage: (Dis)solving the Proteome of Flour and Starch Pastes and Their Adhering Properties.Journal of proteome research · 2024Article
- An Improved Isotope Labelling Method for Quantifying Deamidated Cobratide Using High-Resolution Quadrupole-Orbitrap Mass Spectrometry.Molecules (Basel, Switzerland) · 2022Article
- Spontaneous Cleavages of a Heterologous Protein, the CenA Endoglucanase ofMicrobiology insights · 2021Article
- Evolution of Protein Structure and Stability in Global Warming.International journal of molecular sciences · 2020Review
- Deamidated Human Triosephosphate Isomerase is a Promising Druggable Target.Biomolecules · 2020Article
- Analysis of Glutamine Deamidation: Products, Pathways, and Kinetics.Analytical chemistry · 2019Article
- 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
- Radical solutions: Principles and application of electron-based dissociation in mass spectrometry-based analysis of protein structure.Mass spectrometry reviews · 2018Review
- Replacing HChemical science · 2018Article
- The flexibility and dynamics of protein disulfide isomerase.Proteins · 2016Article
- 2D FT-ICR MS of Calmodulin: A Top-Down and Bottom-Up Approach.Journal of the American Society for Mass Spectrometry · 2016Article
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5 authors.
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Abstract
Deamidation is a nonenzymatic post-translational modification of asparagine to aspartic acid or glutamine to glutamic acid, converting an uncharged amino acid to a negatively charged residue. It is plausible that deamidation of asparagine and glutamine residues would result in disruption of a proteins' hydrogen bonding network and thus lead to protein unfolding. To test this hypothesis Calmodulin and B2M were deamidated and analyzed using tandem mass spectrometry on a Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS). The gas phase hydrogen bonding networks of deamidated and nondeamidated protein isoforms were probed by varying the infra-red multi-photon dissociation laser power in a linear fashion and plotting the resulting electron capture dissociation fragment intensities as a melting curve at each amino acid residue. Analysis of the unfolding maps highlighted increased fragmentation at lower laser powers localized around heavily deamidated regions of the proteins. In addition fragment intensities were decreased across the rest of the proteins which we propose is because of the formation of salt-bridges strengthening the intramolecular interactions of the central regions. These results were supported by a computational flexibility analysis of the mutant and unmodified proteins, which would suggest that deamidation can affect the global structure of a protein via modification of the hydrogen bonding network near the deamidation site and that top down FTICR-MS is an appropriate technique for studying protein folding.
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