Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA.
Nat Struct Mol Biol. 2011 Apr;18(4):504-6. doi: 10.1038/nsmb.2035. Epub 2011 Mar 27.
One of the mysteries in prion research is the structure of the infectious form of mammalian prion protein PrP(Sc). Here we used mass spectrometry analysis of hydrogen-deuterium exchange to examine brain-derived PrP(Sc). Our data indicate that, contrary to popular models, prion-protein conversion involves refolding of the entire region from residue ~80-90 to the C-terminus, which in PrP(Sc) consists of β-strands and relatively short turns and/or loops, with no native α-helices present.
朊病毒研究中的一个谜团是感染性哺乳动物朊病毒蛋白 PrP(Sc)的结构。在这里，我们使用氢氘交换的质谱分析来研究脑源性 PrP(Sc)。我们的数据表明，与流行的模型相反，朊病毒蛋白的转化涉及从残基~80-90 到 C 末端的整个区域的重折叠，在 PrP(Sc)中，该区域由β-链和相对较短的转角和/或环组成，没有天然的α-螺旋存在。
