ArticleProtein science : a publication of the Protein Society2012
Characterization of deamidation of barstar using electrospray ionization quadrupole time-of-flight mass spectrometry, which stabilizes an equilibrium unfolding intermediate.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Elucidating the Degradation Pathways of Human Insulin in the Solid State.Journal of analysis and testing · 2024Article
- In Silico Prediction Method for Protein Asparagine Deamidation.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Sequence and Solution Effects on the Prevalence of d-Isomers Produced by Deamidation.ACS chemical biology · 2017Article
- Deamidation Slows Curli Amyloid-Protein Aggregation.Biochemistry · 2017Article
- Protein asparagine deamidation prediction based on structures with machine learning methods.PloS one · 2017Article
- Engineering deamidation-susceptible asparagines leads to improved stability to thermal cycling in a lipase.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Deamidation of asparaginyl residues is a common posttranslational modification in proteins and has been studied extensively because of its important biological effects, such as those on enzymatic activity, protein folding, and proteolytic degradation. However, characterization of the sites of deamidation of a protein has been a difficult analytical problem. In this study, mass spectrometry has been used as an analytical tool to characterize the deamidation of barstar, an RNAse inhibitor. Upon incubation of the protein at alkaline pH for 5 h, intact mass analysis of barstar, using electrospray ionization quadrupole time-of-flight mass spectrometry (ESI QToF MS), indicated an increase in the mass of +2 Da, suggesting possible deamidation of the protein. The sites of deamidation have been identified using the conventional bottom-up approach using a capillary liquid chromatography connected on line to an ESI QToF mass spectrometer and top down approach by direct infusion of the intact protein and fragmenting inside MS. These chemical modifications are shown to lead to stabilization of an unfolding intermediate, which can be observed in equilibrium unfolding studies.
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