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.