RiAFP: Difference between revisions
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== Ice Binding Surface (IBS) == | == Ice Binding Surface (IBS) == | ||
[[Image:Fig4_D.jpg|frame|alt=Puzzle globe|Fig. 3. Ice-binding surface]] | [[Image:Fig4_D.jpg|frame|alt=Puzzle globe|Fig. 3. Ice-binding surface]] | ||
IBS of RiAFP contains five expanded <scene name='60/607864/Ibs/1'>TXTXTXT motifs</scene> within the top β–sheet. These motifs are remarkably regular, allowing any rows/columns of TXTXTXT motifs to be exactly superposed onto any other rows/columns. Threonine residuses are crucial for maintaining antifreeze activity. It was found in other AFPs that mutations of the Thrs within these motifs decrease the thermal hysteresis. The Thr hydroxyls define a large flat IBS of 420 Å2, which correlates with high antifreeze activity (see Figure 3). | IBS of RiAFP contains five expanded <scene name='60/607864/Ibs/1'>TXTXTXT motifs</scene> within the top β–sheet. These motifs are remarkably regular, allowing any rows/columns of <scene name='60/607864/Isosurface/3'>TXTXTXT motifs</scene> to be exactly superposed onto any other rows/columns. Threonine residuses are crucial for maintaining antifreeze activity. It was found in other AFPs that mutations of the Thrs within these motifs decrease the thermal hysteresis. The Thr hydroxyls define a large flat IBS of 420 Å2, which correlates with high antifreeze activity (see Figure 3). | ||
== Molecular Basis for Ice Binding == | == Molecular Basis for Ice Binding == | ||
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== Function == | == Function == | ||
