ISIS Neutron and Muon Source Data Journal

Unravelling the thermal denaturation and stability of the solution structures of industrially-important antibodies with and without glycans

Abstract: The glycosylation of glycoproteins is a major determinant of their stability, and glycans also affect their aggregatibility (precipitation). An understanding of this is essential for improving manufacturing processes. Our extensive background in glycosylation and scattering (see below) indicates that we are ideally positioned to investigate antibody glycan structures in detail. Our overall aim is to identify how the solution properties of glycans affect antibody manufacture. Following our successful comparison of glycosylated and deglycosylated IgG antibodies by neutron and X-ray scattering and ultracentrifugation, we are now performing their atomistic modelling. In this proposal, to identify the consequences of deglycosylation on stability, we request neutron scattering data to study the structures of deglycosylated antibodies at higher temperatures during denaturation experiments.

Principal Investigator: Professor Stephen Perkins
Experimenter: Miss Valentina Spiteri
Local Contact: Dr James Doutch

DOI: 10.5286/ISIS.E.RB1910550

ISIS Experiment Number: RB1910550

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Professor Stephen Perkins et al; (2019): Unravelling the thermal denaturation and stability of the solution structures of industrially-important antibodies with and without glycans, STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1910550

Data is released under the CC-BY-4.0 license.