从α1链的一级结构角度解读胶原蛋白的小角X射线衍射。
Interpretation of the small-angle X-ray diffraction of collagen in view of the primary structure of the alpha1 chain.
作者信息
Claffey W
出版信息
Biophys J. 1977 Jul;19(1):63-70. doi: 10.1016/S0006-3495(77)85562-8.
Abstract
The small-angle X-ray diffraction pattern of collagen has been calculated using the sequence of the alpha 1 chain and a Hodge-Petruska scheme for the packing of the collagen molecules. The molecular stagger giving the best fit of calculated-to observed structure factors has been found to be 236 or 237 amino acid residues for three tendon collagens. But this result depends on the appoximation that the molecular conformation is uniform throughout the molecule. A comparison of the observed and calculated electron density profiles in axial projection leads to a corrected model, in which the COOH-terminal telopeptide is contracted in a way suggesting a saddle-shaped electron density distribution near the collagenase site.
摘要
利用α1链的序列和霍奇-彼得鲁斯卡胶原蛋白分子堆积模型，计算出了胶原蛋白的小角X射线衍射图谱。对于三种肌腱胶原蛋白，已发现使计算得到的结构因子与观察到的结构因子最佳拟合的分子交错为236或237个氨基酸残基。但该结果取决于分子构象在整个分子中是均匀的这一近似。对轴向投影中观察到的和计算出的电子密度分布进行比较，得到了一个校正模型，其中COOH末端端肽以一种表明在胶原酶位点附近呈鞍形电子密度分布的方式收缩。
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