| Literature DB >> 30462348 |
Linda Cerofolini1, Stefano Giuntini1,2, Azzurra Carlon1, Enrico Ravera1,2, Vito Calderone1,2, Marco Fragai1,2, Giacomo Parigi1,2, Claudio Luchinat1,2.
Abstract
Resonance assignment and structural characterization of pharmacologically relevant proteins promise to improve understanding and safety of these proteins by rational design. However, the PEG coating that is used to evade the immune system also causes these molecules to "evade" the standard structural biology methodologies. We here demonstrate that it is possible to obtain the resonance assignment and a reliable structural model of large PEGylated proteins through an integrated approach encompassing NMR and X-ray crystallography.Entities:
Keywords: PEGylation; biopharmaceuticals; protein modifications; protein structures; structural biology
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Year: 2019 PMID: 30462348 DOI: 10.1002/chem.201804488
Source DB: PubMed Journal: Chemistry ISSN: 0947-6539 Impact factor: 5.236