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"Location of surface waters reveals how antifreeze and ice nucleation proteins 
work."



Peter L. Davies



Department of Biomedical and Molecular Sciences

Queen’s University, Kingston, Ontario, Canada



JULY 30, 13:30(EDT)



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Abstract: Antifreeze proteins that protect marines fishes from freezing in icy 
seawater were discovered in the late 1960’s. They function by binding to 
internal seed ice crystals and preventing their growth. Since then, the variety 
and roles of ice-binding proteins have increased to include the inhibition of 
ice recrystallization, ice adhesion, and even ice nucleation. The mechanism by 
which ice-binding proteins can be freely soluble at millimolar concentrations 
in water and yet bind irreversibly to the ice – the solid state of water – was 
a mystery for a long time. But high resolution crystal structures obtained at 
Brookhaven for several ice-binding proteins showed that they have a clathrate 
water pattern on their ice-binding sites. We now think that these ice-like 
waters merge with the quasi-liquid layer of water around an ice crystal and 
become frozen together at subzero temperatures. Although these proteins are 
only bound to ice by hydrogen bonds and other weak forces, there are many of 
them, and almost all would have to break at the same time for the protein to 
come off the ice. Modeling of ice nucleation protein structures suggests that 
they resemble much larger versions of ice-binding proteins. In addition, they 
are also extensively multimerized. Here similar protein surface structures are 
in place to organize ice-like waters, but in such great numbers that they can 
nucleate freezing at high sub-zero temperatures up to -2 ºC.




=================

Vivian Stojanoff, PhD

Education, Training, Outreach

User Program

p 1(631) 344 8375

e [email protected]<mailto:[email protected]>

w https://www.bnl.gov/ps/lifesciences/<https://www.bnl.gov/ps/lsbr/>



Address:

Center for Biomolecular Structure

National Synchrotron Light Source II

Building 745

Brookhaven National Laboratory

Upton NY 11973




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