Perturbation of conformational dynamics of ASCUT-1 from Ascaris lumbricoides by temperature and sodium dodecyl sulfate
Perturbation of conformational dynamics of ASCUT-1 from Ascaris lumbricoides by temperature and sodium dodecyl sulfate
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DOI：
10.1023/a:1009431428680
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发表时间：
2000-03-01
影响因子：
2.7
通讯作者：
Lakowicz, JR
中科院分区：
文献类型：
--
作者：
D'Auria, S;Bazzicalupo, P;Lakowicz, JR
ASCUT-1是在角质蛋白中发现的蛋白质，角质蛋白是蛔虫线虫的角质蛋白的不溶性残留物。它含有CUT-1样结构域，该结构域由细胞外基质组分的新家族的成员共享。ASCUT-1的单体形式含有单个色氨酸残基。了解蛋白质在不同化学-物理条件下的结构-功能关系对于理解其在细胞中的结构和功能具有重要意义。本文报道了温度和十二烷基硫酸钠对该蛋白结构稳定性的影响。蛋白质的结构进行了研究，在温度范围25-85摄氏度的情况下，在十二烷基硫酸钠的存在下，通过频域测量的固有荧光强度和各向异性衰减。时间分辨的荧光数据表明，在SDS的情况下，dahanyl发射衰减很好地描述了双峰寿命分布，和温度的升高导致的锐化和dahanyl寿命分布的缩短。在SDS的存在下，单峰的荧光寿命分布以及各向异性衰减值显着减少进行了观察。
ASCUT-1 is a protein found in cuticlin, the insoluble residue of the cuticles of the nematode Ascaris lumbricoides. It contains the CUT-1-like domain which is shared by members of a novel family of components of extracellular matrices. The monomeric form of ASCUT-1 contains a single tryptophan residue. An understanding of the structure-function relationship of the protein under different chemical-physical conditions is of fundamental importance for an understanding of its structure and function in cuticles. In this paper we report the effect of the temperature and sodium dodecyl sulfate on the structural stability of this protein. The structure of the protein was studied in the temperature range 25-85 degrees C in the absence and in the presence of sodium dodecyl sulfate by frequency-domain measurements of the intrinsic fluorescence intensity and anisotropy decays. The time-resolved fluorescence data in the absence of SDS indicated that the tryptophanyl emission decays were well described by a bimodal lifetime distribution, and that the temperature increases resulted in the sharpening and in the shortening of the tryptophanyl lifetime distribution. In the presence of SDS an unimodal fluorescence lifetime distribution as well as a marked decrease in the anisotropy decay values were observed.