RiAFP: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 11: | Line 11: | ||
== Ice Binding Surface (IBS) == | == Ice Binding Surface (IBS) == | ||
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. | [[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). | |||
| Line 26: | Line 27: | ||
[[Image:Fig2_C.jpg|frame|alt=Puzzle globe|Fig. 2. Hydrophobicity of RiAFP]] | [[Image:Fig2_C.jpg|frame|alt=Puzzle globe|Fig. 2. Hydrophobicity of RiAFP]] | ||
