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首页> 外文期刊>Spectrochimica acta, Part A. Molecular and biomolecular spectroscopy >New insights in the conformation of #alpha#_1-acid glycoprotein (orosomucoid). Quenching resolved emission anisotropy studies
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New insights in the conformation of #alpha#_1-acid glycoprotein (orosomucoid). Quenching resolved emission anisotropy studies

机译：＃alpha＃_1-酸性糖蛋白（类骨粉）构象的新见解。淬火分解发射各向异性研究

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摘要

Quenching resolved emission anisotropy method was applied to study the dynamics of the two classes of Trp residues of human #alpha#_1-acid glycoprotein (orosomucoid), in the absence and presence of progesterone. In the absence of progesterone, the values of the anisotropies of the surface and buried Trp residues are 0.155 and 0.178, respectively. These values lower than the limiting anisotropy (0,267) indicate that both classes of Trp residues display residual motions. In the presence of progesterone, the values of the anisotropies decrease from 0.155 to 0.146 and from 0.178 to 0.167. Thus, binding of progesterone to orosomucoid increases the internal dynamics of the protein. Also, the fact that in the absence or in the presence of progesterone, the anisotropies of both classes are close, means that the amplitudes of the motions of the two classes are not significantly different. From our data and from the well-known position of the carbohydrate residues on orosomucoid, we suggest the presence of a hydrophobic pocket within the protein and where the 'buried' Trp residues can be found.
机译：在没有孕酮存在的情况下，采用淬灭分辨发射各向异性方法研究了人类＃α＃_1-酸糖蛋白（类类固醇）的两类Trp残基的动力学。在没有孕酮的情况下，表面和掩埋的Trp残基的各向异性值分别为0.155和0.178。这些低于极限各向异性（0,267）的值表明，这两种Trp残基都显示出残余运动。在孕酮存在下，各向异性值从0.155降低到0.146，从0.178降低到0.167。因此，黄体酮与类骨粉的结合增加了蛋白质的内部动力学。同样，在不存在或存在孕酮的情况下，两类的各向异性都接近，这一事实意味着两类运动的幅度没有显着差异。根据我们的数据以及糖类类固醇上碳水化合物残基的已知位置，我们建议蛋白质中存在疏水口袋，并且可以在其中发现“埋藏”的Trp残基。

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