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Biophys J, May 1998, p. 2142-2151, Vol. 74, No. 5
*Department of Biochemistry, Faculty of Health Science, McMaster University, Hamilton, Ontario L8N 3Z5, Canada; #BioCrystallography Laboratory, VA Medical Centre, Pittsburgh, Pennsylvania 15240 USA; and §Research Institute, Hospital for Sick Children, Toronto, and Departments of Clinical Biochemistry and Biochemistry, University of Toronto, Toronto, Ontario M5G 1L5, Canada
Antifreeze proteins (AFPs) adsorb to surfaces of growing
ice crystals, thereby arresting their growth. The prevailing hypothesis explains the nature of adsorption in terms of a match between the
hydrophilic side chains on the AFP's ice-binding surface (IBS) and the
water molecules on the ice surface. The number and spatial arrangement
of hydrogen bonds thus formed have been proposed to account,
respectively, for the binding affinity and specificity. The crystal
structure of a type III AFP from ocean pout (isoform HPLC-3) has been
determined to 2.0-Å resolution. The structure reveals an internal dyad
motif formed by two 19-residue, loop-shaped elements. Based on of the
flatness observed on the type I 
-helical AFP's IBS, an automated
algorithm was developed to analyze the surface planarity of the
globular type III AFP and was used to identify the IBS on this protein.
The surface with the highest flatness score is formed by one loop of
the dyad motif and is identical to the IBS deduced from earlier
mutagenesis studies. Interestingly, 67% of this surface contains
nonpolar solvent-accessible surface area. The success of our approach
to identifying the IBS on an AFP, without considering the presence of
polar side chains, indicates that flatness is the first approximation
of an IBS. We further propose that the specificity of interactions
between an IBS and a particular ice-crystallographic plane arises from surface complementarity.
Biophys J, May 1998, p. 2142-2151, Vol. 74, No. 5
© 1998 by the Biophysical Society 0006-3495/98/05/2142/10 $2.00
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