A root bond between ice and antifreeze protein

被引:7
作者
Hawes, Timothy C. [1 ]
机构
[1] Khon Kaen Univ, Int Coll, 123 Mitraphap Highway, Khon Kaen 40002, Thailand
关键词
Amino acid; Antifreeze protein; Denaturation; Ice-binding; BEETLE DENDROIDES-CANADENSIS; THERMAL HYSTERESIS; ADSORPTION; MECHANISM; PURIFICATION; ENHANCEMENT; PEPTIDES; BINDING; SURFACE; FISHES;
D O I
10.1016/j.cryobiol.2016.08.007
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
It has always been assumed that a three-dimensional protein structure is essential to antifreeze protein (AFP) ice interactions. Using a 9 kDa AFP isolated from the springtail, Gomphiocephalus hodgsoni, it was found that the bond between ice and protein is maintained independent of higher order protein structure. GomplyAFP(9) remained bound to ice after denaturing by a range of agents (boiling, extreme pH, DTT, ethanol, urea). Thermal hysteresis was minimal (0.03-0.04 degrees C), but not lost. Crystal faceting and growth occurred normal to the c-axis, indicating the protein binds primarily to sites along the a-axis. These observations lend additional support to the hypothesis of irreversible binding. More significantly, they suggest that binding to ice and functional hysteresis may be achieved independently (i.e. are different operations). These results are consistent with the view that there is a root bond with ice and it is achieved via an amino acid derived interface that bonds to water molecules in aqueous solutions. (C) 2016 Elsevier Inc. All rights reserved.
引用
收藏
页码:147 / 151
页数:5
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