ArticleMolecular & cellular proteomics : MCP2012
Mapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probe.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Mass spectrometry-complemented molecular modeling predicts the interaction interface for a camelid single-domain antibody targeting theComputational and structural biotechnology journal · 2024Article
- Evaluating the performance of an ETD-cleavable cross-linking strategy for elucidating protein structures.Journal of proteomics · 2020Article
- The Role of Electron Transfer Dissociation in Modern Proteomics.Analytical chemistry · 2018Review
- Exploitation of the Ornithine Effect Enhances Characterization of Stapled and Cyclic Peptides.Journal of the American Society for Mass Spectrometry · 2016Article
- High-throughput bioconjugation for enhanced 193 nm photodissociation via droplet phase initiated ion/ion chemistry using a front-end dual spray reactor.Analytical chemistry · 2015Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
A protein's surface influences its role in protein-protein interactions and protein-ligand binding. Mass spectrometry can be used to give low resolution structural information about protein surfaces and conformations when used in combination with derivatization methods that target surface accessible amino acid residues. However, pinpointing the resulting modified peptides upon enzymatic digestion of the surface-modified protein is challenging because of the complexity of the peptide mixture and low abundance of modified peptides. Here a novel hydrazone reagent (NN) is presented that allows facile identification of all modified surface residues through a preferential cleavage upon activation by electron transfer dissociation coupled with a collision activation scan to pinpoint the modified residue in the peptide sequence. Using this approach, the correlation between percent reactivity and surface accessibility is demonstrated for two biologically active proteins, wheat eIF4E and PARP-1 Domain C.
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