RiAFP
From Proteopedia
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== 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). | ||
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[[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]] | ||
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- | [[Image:Fig4_D.jpg|frame|alt=Puzzle globe|Fig. 3. Ice-binding surface]] | ||
Revision as of 23:29, 24 January 2015
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3D structures of antifreeze protein
References
- ↑ Jia Z, Davies PL. Antifreeze proteins: an unusual receptor-ligand interaction. Trends Biochem Sci. 2002 Feb;27(2):101-6. PMID:11852248
- ↑ Chantelle J. Capicciotti, Malay Doshi and Robert N. Ben (2013). Ice Recrystallization Inhibitors: From Biological Antifreezes to Small Molecules, Recent Developments in the Study of Recrystallization, Prof. Peter Wilson (Ed.), ISBN: 978-953-51-0962-4, InTech doi:http://dx.doi.org/10.5772/54992
- ↑ Drori R, Celik Y, Davies PL, Braslavsky I. Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics. J R Soc Interface. 2014 Sep 6;11(98):20140526. doi: 10.1098/rsif.2014.0526. PMID:25008081 doi:http://dx.doi.org/10.1098/rsif.2014.0526
- ↑ doi: https://dx.doi.org/10.1016/S0006-3495(91)82234-2
- ↑ Hakim A, Nguyen JB, Basu K, Zhu DF, Thakral D, Davies PL, Isaacs FJ, Modis Y, Meng W. Crystal structure of an insect antifreeze protein and its implications for ice binding. J Biol Chem. 2013 Apr 26;288(17):12295-304. doi: 10.1074/jbc.M113.450973. Epub, 2013 Mar 12. PMID:23486477 doi:10.1074/jbc.M113.450973