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Instability of buried hydration sites increases protein subdomains fluctuations in the human prion protein by the pathogenic mutation T188R

机译：埋藏水合位点的不稳定性通过致病突变T188R增加人朊病毒蛋白中的蛋白质亚结构域波动

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Katsufumi Tomobe; Eiji Yamamoto; Takuma Akimoto; Masato Yasui; Kenji Yasuoka;
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1. Instability of buried hydration sites increases protein subdomains fluctuations in the human prion protein by the pathogenic mutation T188R [J] . Katsufumi Tomobe, Eiji Yamamoto, Takuma Akimoto, AIP Advances . 2016,第5期

机译：埋藏的水合位点的不稳定性通过致病性突变T188R增加了人类病毒蛋白的蛋白质亚域波动
2. Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding. [J] . van der Kamp MW, Daggett V Journal of Molecular Biology . 2010,第4期

机译：人类病毒蛋白疏水核心的致病突变可促进结构不稳定和错误折叠。
3. Human prion proteins with pathogenic mutations share common conformational changes resulting in enhanced binding to glycosaminoglycans [J] . Shaoman Yin, Nancy Pham, Shuiliang Yu, Proceedings of the National Academy of Sciences of the United States of America . 2007,第18期

机译：具有致病性突变的人类病毒蛋白具有共同的构象变化，从而增强了与糖胺聚糖的结合
4. Molecular dynamics simulations to study pathogenic mutations in proteins [C] . Valentina Mirabelli, Rocco Caliandro, Giovanni Nico, IMEKO TC4 Symposium Measurements of Electrical Quantities . 2014

机译：分子动力学模拟研究蛋白质致病性突变
5. Elucidating the Effect of Myopathy-causing Mutations and Second-site Suppressors on Client Processing by J-Domain Proteins [D] . ?Pullen-Colon, Melanie Yaines 2020

机译：阐明肌病引起的突变和第二位点抑制对J-域蛋白的客户处理的影响
6. Pathogenic mutations in the hydrophobic core of the human prion protein can promote structural instability and misfolding [O] . Marc W. van der Kamp, Valerie Daggett -1

机译：在人朊蛋白的疏水核心致病突变可促进结构不稳定和错误折叠
7. 2P130 Water behavior in buried hydration sites of human cellular prion protein and pathogenic mutation T188R(07. Water Hydration Electrolyte,Poster) [O] . Katsufumi Tomobe, Eiji Yamamoto, Takuma Akimoto, 2013

机译：2P130人体细胞朊病毒蛋白和致病性突变的埋藏水合位点的水行为T188R（07.水和水合和电解质，海报）

Instability of buried hydration sites increases protein subdomains fluctuations in the human prion protein by the pathogenic mutation T188R

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