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Unusual property of prionprotein unfolding in neutral salt solution

机译：neutral蛋白在中性盐溶液中展开的异常性质

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摘要

The unfolding of cellular prion protein and its refolding to the scrapie isoform are related to prion diseases.Studies in the literature have shown that structures of proteins,either acidic or basic,are stabilized against denaturation by certainneutral salts,for example,sulfate and fluoride.Contrary to these observations,the full-length recombinant prion protein (amino acid residues 23-231) is denatured by these protein structure stabilizing salts.Under identical concentrations of salts,teh structure of the sheep prionprotein,which contains a greater number of glycine groups in the N-terminal unstructured segment than the mouse protein,becomes more destabilized.In contrast to the full-length protein,the C-terminal 121-231 prion protein fragment,consisting of all the structural elements of the protein,viz.,three alpha-helices and two short beta-strands,is stabilized against denaturation by these salts.We suggest that an increase in the concentration of the anions on the surface of the prion protein molecule due to their preferential interaction with the glycine residues in the N-terminal segment destabilizes the structure of the prion protein by perturbing the prion helix 1 which is the most soluble of all the protein alpha-helices reported so far in the literature.The present results could be relevant to explain the observed structural conversion of the prion protein by anionic nucleic acid and sulfated glycosaminoglycans.
机译：细胞病毒蛋白的解折叠及其向瘙痒病亚型的复性与病毒疾病有关。文献研究表明，酸性或碱性蛋白质的结构对某些中性盐（例如硫酸盐和氟化物）的变性具有稳定作用。与这些观察结果相反，全长重组病毒蛋白（氨基酸残基23-231）被这些蛋白质结构稳定盐变性。在相同浓度的盐下，绵羊病毒蛋白的结构具有更大的甘氨酸基团与小鼠蛋白质相比，在N末端非结构化片段中的稳定性更不稳定。与全长蛋白质相反，C末端121-231 pr病毒蛋白质片段由该蛋白质的所有结构组成，即三个这些盐稳定了α-螺旋和两个短的β-链的抗变性。我们建议增加p表面上阴离子的浓度rion蛋白分子由于其与N末端区段中的甘氨酸残基的优先相互作用而扰乱了prion helix 1，从而破坏了prion蛋白的结构，而prion helix 1是迄今为止在文献中报道的所有蛋白质α-螺旋中最易溶的。目前的结果可能与解释阴离子核酸和硫酸化糖胺聚糖对ans病毒蛋白的结构转化有关。

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