Selective suppression of excipient signals in 2D 1H–13C methyl spectra of biopharmaceutical products
Author:
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/article/10.1007/s10858-018-0214-1/fulltext.html
Reference25 articles.
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2. Arbogast LW, Brinson RG, Marino JP (2015) Mapping monoclonal antibody structure by 2D 13 C NMR at natural abundance. Anal Chem 87:3556–3561
3. Arbogast LW, Brinson RG, Marino JP (2016a) Application of natural isotopic abundance 1H–13C- and 1H–15N-correlated two-dimensional NMR for evaluation of the structure of protein therapeutics. Methods Enzymol 566:3–34
4. Arbogast LW, Brinson RG, Formolo T, Hoopes JT, Marino JP (2016b) 2D 1HN, 15N correlated NMR methods at natural abundance for obtaining structural maps and statistical comparability of monoclonal antibodies. Pharm Res 33:462–475
5. Arbogast LW, Delaglio F, Schiel JE, Marino JP (2017) Multivariate analysis of two-dimensional 1H, 13C Methyl NMR spectra of monoclonal antibody therapeutics to facilitate assessment of higher order structure. Anal Chem 89:11839–11845
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