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Mathematical Formulas for Prion All Cross-Structures Listed in the Protein Data Bank

机译:蛋白质数据库中列出的Prion所有交叉结构的数学公式

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Prion protein (PrP) has two regions: unstructured region PrP(1-120) and structured region PrP(119-231). In the structured region, there are many segments which have the property of amyloid fibril formation. By theoretical calculations, PrP(126-133), PrP(137-143), PrP(170-175), PrP(177-182), PrP(211-216) have the amyloid fibril forming property. PrP(142-166) has a X-ray crystallography experimental β-hairpin structure, instead of a pure cross-β amyloid fibril structure; thus we cannot clearly find it by our theoretical calculations. However, we can predict that there must be a laboratory X-ray crystal structure in PrP(184-192) segment that will be produced in the near future. The experiments of X-ray crystallography laboratories are agreeing with our theoretical calculations. This article summarized mathematical formulas of prion amyloid fibril cross-β structures of all the above PrP segments currently listed in the Protein Data Bank.
机译:on病毒蛋白(PrP)具有两个区域:非结构化区域PrP(1-120)和结构化区域PrP(119-231)。在结构化区域中,存在许多具有淀粉样蛋白原纤维形成特性的区段。通过理论计算,PrP(126-133),PrP(137-143),PrP(170-175),PrP(177-182),PrP(211-216)具有淀粉样原纤维形成特性。 PrP(142-166)具有X射线晶体学实验的β-发夹结构,而不是纯的交叉β-淀粉样蛋白原纤维结构;因此我们无法通过理论计算清楚地找到它。但是,我们可以预测在不久的将来将在PrP(184-192)段中存在一个实验室X射线晶体结构。 X射线晶体学实验室的实验与我们的理论计算相符。本文总结了蛋白质数据库中目前列出的所有上述PrP片段的ion病毒淀粉样蛋白原纤维交叉β结构的数学公式。

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