Coming upTue 3 Nov 2026,
Ice-philicity, Ice Binding, and Ice Recrystallization Inhibition By Antifreeze Proteins
Natural antifreeze proteins, and how they cling to ice crystals to stop them from growing and damaging frozen tissues.
The defense
From the University of Pennsylvania agenda
- When
- Tue 3 Nov 2026, 90 min
- Where
- University of Pennsylvania, United StatesChemical and Biomolecular Engineering
- Fields
- Supervisor
- Jury
- Daeyeon LeeCBEdblp
- Talid SinnoCBEdblp
- Kim SharpBiochemistry and Biophysics
- Language
- English
- Stream
- on Zoom
Stream link
A doctoral defense is public: anyone may watch.
From the abstract
Antifreeze proteins enable cold-adapted organisms to manage ice crystal growth by attaching directly to crystal surfaces. This surface binding halts crystal expansion and prevents recrystallization, a destructive process where larger ice crystals consume smaller ones in frozen foods and cryopreserved tissues. The research addresses two unresolved issues concerning these proteins. First, locating an ice-binding site remains difficult because these regions often lack obvious structural features, requiring laborious residue-by-residue mutagenesis. Second, while antifreeze proteins are known to halt the growth and melting of individual crystals, the mechanism by which they suppress recrystallization throughout a collective population of crystals remains unknown.
Is this your defense?
Write the featured defense page: an opening, a pull quote, and three questions. Sending it for review claims the defense as yours.
Listed from the University of Pennsylvania agenda.