Conformational Stability of Syrian Hamster Prion Protein PrP(90-231)
Conformational Stability of Syrian Hamster Prion Protein PrP(90-231)
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DOI：
10.1021/ja100243h
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发表时间：
2010-07-07
影响因子：
15
通讯作者：
Bowers, Michael T.
中科院分区：
文献类型：
--
作者：
Grabenauer, Megan;Wyttenbach, Thomas;Bowers, Michael T.
许多传染性海绵状脑病（TSE）被认为是由正常细胞朊蛋白（PrPC）的错误折叠形式（称为PrPSc）引起的。虽然已知PrPSc非常稳定且对蛋白酶降解具有抗性，但PrPC并未显示出这些相同的不寻常特征。然而，使用离子迁移谱质谱法（IMS-MS），我们发现的证据，至少有一个非常稳定的构象的截断形式的重组PrPC组成的残基90 - 231，抵抗展开在没有溶剂的情况下，在高注射能量和温度超过600 K。我们还报告了重组叙利亚仓鼠朊蛋白PrP（90 - 231）测量的第一个绝对碰撞截面。
Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrPC) known as PrPSc. While PrPSc is known to be exceptionally stable and resistant to protease degradation, PrPC has not shown these same unusual characteristics. However, using ion mobility spectrometry mass spectrometry (IMS-MS), we found evidence for at least one very stable conformation of a truncated form of recombinant PrPC consisting of residues 90-231, which resists unfolding in the absence of solvent at high injection energies and at temperatures in excess of 600 K. We also report the first absolute collision cross sections measured for recombinant Syrian hamster prion protein PrP(90-231).