朊病毒AGAAAAGA淀粉样纤维的最佳原子分辨结构
Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils
摘要：
X射线晶体学是确定蛋白质3D结构的有力工具。然而，这是耗时和昂贵的，并不是所有的蛋白质都可以成功地结晶，特别是膜蛋白。虽然核磁共振（NMR）光谱确实是确定膜蛋白3D结构的一个非常强大的工具，但它也是耗时和昂贵的。据作者所知，由于淀粉样原纤维的非结晶和不溶性，朊病毒蛋白疏水区（113-120）中的AGAAAAGA回文结构数据很少，尽管许多实验研究表明该区域具有淀粉样原纤维形成特性，并在朊病毒疾病中起重要作用。鉴于此，本研究致力于解决这个问题，从计算方法，如全局能量优化，模拟退火，结构生物信息学。本文报道的朊病毒AGAAAAGA淀粉样蛋白的最佳原子分辨率结构对科学界寻找朊病毒疾病的治疗方法具有价值。
英文摘要：
X-ray crystallography is a powerful tool to determine the protein 3D structure. However, it is time-consuming and expensive, and not all proteins can be successfully crystallized, particularly for membrane proteins. Although nuclear magnetic resonance (NMR) spectroscopy is indeed a very powerful tool in determining the 3D structures of membrane proteins, it is also time-consuming and costly. To the best of the authors' knowledge, there is little structural data available on the AGAAAAGA palindrome in the hydrophobic region (113-120) of prion proteins due to the noncrystalline and insoluble nature of the amyloid fibril, although many experimental studies have shown that this region has amyloid fibril forming properties and plays an important role in prion diseases. In view of this, the present study is devoted to address this problem from computational approaches such as global energy optimization, simulated annealing, and structural bioinformatics. The optimal atomic-resolution structures of prion AGAAAAGA amyloid fibils reported in this paper have a value to the scientific community in its drive to find treatments for prion diseases.
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