Methodology for Determining Disulfide Linkage Patterns of Closely Spaced Cysteine Residues
Author:
Affiliation:
1. Analytical Sciences, Amgen, Inc., 4000 Nelson Road, Longmont, Colorado 80503
Publisher
American Chemical Society (ACS)
Subject
Analytical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ac901161e
Reference18 articles.
1. Role of disulfide bridges in the folding, structure and biological activity of ω-conotoxin GVIA
2. Structural and Functional Characterization of Disulfide Isoforms of the Human IgG2 Subclass
3. Determination of the Disulfide Structure of Sillucin, a Highly Knotted, Cysteine-Rich Peptide, by Cyanylation/Cleavage Mass Mapping
4. Disulfide Connectivity of Human Immunoglobulin G2 Structural Isoforms
5. Characterization of cysteine residues and disulfide bonds in proteins by liquid chromatography/electrospray ionization tandem mass spectrometry
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