...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Unusual property of prion protein unfolding in neutral salt solution.
【24h】

Unusual property of prion protein unfolding in neutral salt solution.

机译：neutral病毒蛋白在中性盐溶液中展开的异常特性。

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

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 certain neutral 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, the structure of the sheep prion protein, 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 acids 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可通过某些中性盐（例如硫酸盐和氟化物）稳定而不会变性。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than病毒蛋白的结构变得更加不稳定，该蛋白在N端非结构化片段中包含更多的甘氨酸基团。与全长蛋白质相反，由这些蛋白质的所有结构元素组成的C端121-231 ion病毒蛋白质片段稳定了，以防止变性，这些片段包括三个α螺旋和两个短β链。盐。我们认为，由于their蛋白与N末端片段中的甘氨酸残基的优先相互作用，导致the蛋白蛋白分子表面阴离子的浓度增加，这会扰乱the蛋白螺旋1，从而破坏the蛋白的结构。迄今为止，在文献中报道的所有蛋白质α-螺旋中最易溶。本结果可能与解释阴离子核酸和硫酸化糖胺聚糖对glyc病毒蛋白的结构转化有关。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号