γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.
γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.
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DOI：
10.1021/jp509134d
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发表时间：
2014-11-26
期刊：
影响因子：
--
通讯作者：
Martin RW
中科院分区：
文献类型：
--
作者：
Kingsley CN;Bierma JC;Pham V;Martin RW
γS1-和γS2-晶体蛋白是南极洋枪鱼（Dissostichus mawsoni）眼透镜结构蛋白，与人类透镜蛋白γS-crystallin同源。虽然γS1具有较高的热稳定性，但它更容易被尿素化学变性。两种洋枪鱼晶体蛋白相对于人类γ S-晶体蛋白的热力学稳定性较低，这与目前的研究结果一致，即来自常年寒冷环境特有的生物体的蛋白质如何通过更大的结构灵活性实现低温功能。在某些方面，γS1-和γS2-晶状体蛋白的序列是典型的嗜冷蛋白;然而，它们的氨基酸组成也反映了它们对高折射率增量的选择。像他们的同行在人类透镜和那些嗜温鱼类，这两个toothfish晶体蛋白是相对丰富的芳香族残基和蛋氨酸和exiliment在脂肪族残基。有时相互矛盾的要求选择耐寒性和高折射率的toothfish晶体蛋白的一个很好的模型系统，用于进一步研究的生物物理特性的结构蛋白。
The γS1- and γS2-crystallins, structural eye lens proteins from the Antarctic toothfish (Dissostichus mawsoni), are homologues of the human lens protein γS-crystallin. Although γS1 has the higher thermal stability of the two, it is more susceptible to chemical denaturation by urea. The lower thermodynamic stability of both toothfish crystallins relative to human γS-crystallin is consistent with the current picture of how proteins from organisms endemic to perennially cold environments have achieved low-temperature functionality via greater structural flexibility. In some respects, the sequences of γS1- and γS2-crystallin are typical of psychrophilic proteins; however, their amino acid compositions also reflect their selection for a high refractive index increment. Like their counterparts in the human lens and those of mesophilic fish, both toothfish crystallins are relatively enriched in aromatic residues and methionine and exiguous in aliphatic residues. The sometimes contradictory requirements of selection for cold tolerance and high refractive index make the toothfish crystallins an excellent model system for further investigation of the biophysical properties of structural proteins.
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