叙利亚仓鼠朊病毒蛋白 PrP(90-231)的构象稳定性。
Conformational stability of Syrian hamster prion protein PrP(90-231).
机构信息
Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106, USA.
出版信息
J Am Chem Soc. 2010 Jul 7;132(26):8816-8. doi: 10.1021/ja100243h.
Abstract
Many transmissible spongiform encephalopathies (TSEs) are believed to be caused by a misfolded form of the normal cellular prion protein (PrP(C)) known as PrP(Sc). While PrP(Sc) is known to be exceptionally stable and resistant to protease degradation, PrP(C) 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 PrP(C) 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).
摘要
许多传染性海绵状脑病（TSE）被认为是由正常细胞朊病毒蛋白（PrP(C)）的错误折叠形式引起的，这种形式被称为 PrP(Sc)。虽然已知 PrP(Sc)异常稳定，并且对蛋白酶降解具有抗性，但 PrP(C)并未表现出这些相同的异常特征。然而，使用离子淌度谱质谱（IMS-MS），我们发现了至少一种非常稳定的重组 PrP(C)截断形式的构象证据，该形式由残基 90-231 组成，在高注入能量和超过 600 K 的温度下，在没有溶剂的情况下，该形式阻止展开。我们还报告了第一个为重组叙利亚仓鼠朊病毒蛋白 PrP(90-231)测量的绝对碰撞截面。
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