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Ab initio:
GeNMR
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Refinement:
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Structure from chemical shifts:
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Secondary structure from chemical shifts:
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NMR spectrum prediction:
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Molecular dynamics:
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Chemical shifts prediction:
From structure:
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From sequence:
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Disordered proteins:
MAXOCC
Format conversion & validation:
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From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
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Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Old 04-08-2024, 03:06 PM
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Default Assessment of monoclonal antibody glycosylation: a comparative study using HRMS, NMR, and HILIC-FLD

Assessment of monoclonal antibody glycosylation: a comparative study using HRMS, NMR, and HILIC-FLD

Monoclonal antibodies (mAbs) represent the largest class of therapeutic protein drug products. mAb glycosylation produces a heterogeneous, analytically challenging distribution of glycoforms that typically should be adequately characterized because glycosylation-based product quality attributes (PQAs) can impact product quality, immunogenicity, and efficacy. In this study, two products were compared using a panel of analytical methods. Two high-resolution mass spectrometry (HRMS) workflows were...

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