Antifreeze proteins: an unusual receptor–ligand interaction

Z Jia, PL Davies - Trends in biochemical sciences, 2002 - cell.com
Z Jia, PL Davies
Trends in biochemical sciences, 2002cell.com
Antifreeze proteins (AFPs) help organisms to survive below 0° C by inhibiting ice growth.
Although AFPs are structurally diverse, they typically present a large proportion of their
surface area for binding to ice. Whereas earlier proposed binding mechanisms relied almost
entirely on a hydrogen bond match between the AFP and ice, it now seems probable that
van der Waals and hydrophobic interactions make a significant contribution to the enthalpy
of adsorption. These interactions require intimate surface–surface complementarity between …
Abstract
Antifreeze proteins (AFPs) help organisms to survive below 0°C by inhibiting ice growth. Although AFPs are structurally diverse, they typically present a large proportion of their surface area for binding to ice. Whereas earlier proposed binding mechanisms relied almost entirely on a hydrogen bond match between the AFP and ice, it now seems probable that van der Waals and hydrophobic interactions make a significant contribution to the enthalpy of adsorption. These interactions require intimate surface–surface complementarity between the receptor (AFP) and its ligand (ice).
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