NMR Characterizations of the Ice Binding Surface of an Antifreeze   Protein

doi:10.1371/journal.pone.0015682

CORC > 北京大学 > 化学与分子工程学院

	NMR Characterizations of the Ice Binding Surface of an Antifreeze Protein
	Hong, Jiang ; Hu, Yunfei ; Li, Congmin ; Jia, Zongchao ; Xia, Bin ; Jin, Changwen
刊名	plos one
	2010
关键词	GROUP HYDROGEN-EXCHANGE CHEMICAL-SHIFTS SPRUCE BUDWORM FREEZING RESISTANCE TEMPERATURE DYNAMICS RELAXATION WATER RECOGNITION POLYPEPTIDE
DOI	10.1371/journal.pone.0015682
英文摘要	Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of much higher concentration which likely imposes a large kinetic barrier for protein-ice recognition. In this study, we explore this question by investigating the property of the ice binding surface of an antifreeze protein using NMR spectroscopy. An investigation of the temperature gradient of amide proton chemical shift and its correlation with chemical shift deviation from random coil was performed for CfAFP-501, a hyperactive insect AFP. A good correlation between the two parameters was observed for one of the two Thr rows on the ice binding surface. A significant temperature-dependent protein-solvent interaction is found to be the most probable origin for this correlation, which is consistent with a scenario of hydrophobic hydration on the ice binding surface. In accordance with this finding, rotational correlation time analyses combined with relaxation dispersion measurements reveals a weak dimer formation through ice binding surface at room temperature and a population shift of dimer to monomer at low temperature, suggesting hydrophobic effect involved in dimer formation and hence hydrophobic hydration on the ice binding surface of the protein. Our finding of hydrophobic hydration on the ice binding surface provides a test for existing simulation studies. The occurrence of hydrophobic hydration on the ice binding surface is likely unnecessary for enhancing protein-ice binding affinity which is achieved by a tight H-bonding network. Subsequently, we speculate that the hydrophobic hydration occurring on the ice binding surface plays a role in facilitating protein-ice recognition by lowering the kinetic barrier as suggested by some simulation studies.; Multidisciplinary Sciences; SCI(E); PubMed; 1; ARTICLE; 12; e15682; 5
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/344003]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Hong, Jiang,Hu, Yunfei,Li, Congmin,et al. NMR Characterizations of the Ice Binding Surface of an Antifreeze Protein[J]. plos one,2010.
APA	Hong, Jiang,Hu, Yunfei,Li, Congmin,Jia, Zongchao,Xia, Bin,&Jin, Changwen.(2010).NMR Characterizations of the Ice Binding Surface of an Antifreeze Protein.plos one.
MLA	Hong, Jiang,et al."NMR Characterizations of the Ice Binding Surface of an Antifreeze Protein".plos one (2010).