Covalent Labeling with Diethylpyrocarbonate: Sensitive to the Residue Microenvironment, Providing Improved Analysis of Protein Higher Order Structure by Mass Spectrometry
Author:
Affiliation:
1. Department of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts 01003, United States
Funder
National Institutes of Health
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Analytical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.analchem.9b01732
Reference54 articles.
1. Structural Characterization of Short-Lived Protein Unfolding Intermediates by Laser-Induced Oxidative Labeling and Mass Spectrometry
2. Submillisecond Protein Folding Events Monitored by Rapid Mixing and Mass Spectrometry-Based Oxidative Labeling
3. Temperature Jump and Fast Photochemical Oxidation Probe Submillisecond Protein Folding
4. Fast Photochemical Oxidation of Proteins and Mass Spectrometry Follow Submillisecond Protein Folding at the Amino-Acid Level
5. Copper Binding to β-2-Microglobulin and Its Pre-Amyloid Oligomers
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