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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Pressure-temperature folding landscape in proteins involved in neurodegenerative diseases and cancer
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Pressure-temperature folding landscape in proteins involved in neurodegenerative diseases and cancer

机译：涉及神经退行性疾病和癌症的蛋白质的压力-温度折叠景观

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摘要

High hydrostatic pressure (HHP) is a valuable tool to study processes such as protein folding, protein hydra-tion and protein-protein interactions. HHP is a nondestructive technique because it reversibly affects internal cavities excluded from the solvent present in the hydrophobic core of proteins. HHP allows the solvation of buried amino acid side chains, thus shifting the equilibrium towards states of the studied molecule or molecular ensemble that occupy smaller volumes. HHP has long been used to dissociate multimeric proteins and protein aggregates and allows investigation of intermediate folding states, some of which are formed by proteins involved in human degenerative diseases, such as spongiform encephalopathies and Parkinson's disease, as well as cancer. When coupled with nuclear magnetic resonance and spectroscopic methods such as infrared and fluorescence spectroscopy, HHP treatment facilitates the understanding of protein folding and misfolding processes; the latter is related to protein aggregation into amyloid or amorphous species.
机译：高静水压（HHP）是研究蛋白质折叠，蛋白质水合和蛋白质-蛋白质相互作用等过程的宝贵工具。 HHP是一种非破坏性技术，因为它可逆地影响排除在蛋白质疏水核心中的溶剂所排除的内部空腔。 HHP可以使埋藏的氨基酸侧链发生溶剂化，从而使平衡向所研究的分子或分子整体占据较小体积的状态转移。 HHP长期以来一直用于解离多聚体蛋白质和蛋白质聚集体，并允许研究中间折叠状态，其中某些折叠状态是由参与人类变性疾病（例如海绵状脑病和帕金森氏病）以及癌症的蛋白质形成的。当与核磁共振和红外光谱和荧光光谱等光谱方法结合使用时，HHP处理可促进对蛋白质折叠和错误折叠过程的理解。后者与蛋白质聚集成淀粉样蛋白或无定形物质有关。

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