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Posttranslational Modifications of Intact Proteins Detected by NMR Spectroscopy: Application to Glycosylation
Author(s) -
Schubert Mario,
Walczak Michal J.,
Aebi Markus,
Wider Gerhard
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201502093
Subject(s) - glycosylation , glycan , computational biology , nuclear magnetic resonance spectroscopy , chemistry , isotopic labeling , function (biology) , posttranslational modification , biochemistry , biology , glycoprotein , enzyme , genetics , stereochemistry , organic chemistry
Posttranslational modifications (PTMs) are an integral part of the majority of proteins. The characterization of structure and function of PTMs can be very challenging especially for glycans. Existing methods to analyze PTMs require complicated sample preparations and suffer from missing certain modifications, the inability to identify linkage types and thus chemical structure. We present a direct, robust, and simple NMR spectroscopy method for the detection and identification of PTMs in proteins. No isotope labeling is required, nor does the molecular weight of the studied protein limit the application. The method can directly detect modifications on intact proteins without sophisticated sample preparation. This approach is well suited for diagnostics of proteins derived from native organisms and for the quality control of biotechnologically produced therapeutic proteins.