Journal
SOFT MATTER
Volume 10, Issue 23, Pages 4056-4060Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4sm00600c
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Funding
- National Science Foundation [DMR-0944772]
- National Research Council
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Small-angle neutron scattering was employed to study protein crowding under freezing conditions that mimic those used in pharmaceutical processing. The results demonstrate that, although there is an increase in heterogeneity as the temperature is reduced, sorbitol reduces protein crowding in both solution and freeze-concentrated phases, thus protecting the protein from forming oligomers or irreversible aggregates.
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