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首页> 外文会议>ASMS Conference on Mass Spectrometry and Allied Topics >Small Heat Shock Protein/Substrate Interaction Probed by Solution Phase Hydrogen/Deuterium Exchange, Hydroxyl Radical Modification and Mass Spectrometry
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Small Heat Shock Protein/Substrate Interaction Probed by Solution Phase Hydrogen/Deuterium Exchange, Hydroxyl Radical Modification and Mass Spectrometry

机译：通过溶液相氢/氘交换探测的小型热休克蛋白/底物相互作用，羟基自由基改性和质谱

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摘要

The small heat shock proteins (sHsps) and related alpha-crystallins are a class of oligomeric chaperones that have a very large capacity for binding denatured proteins, thereby preventing irreversible protein denaturation/aggregation upon heat stress. In humans, sHsps have been related to muscle diseases, certain cancers and neurodegenerative diseases. Despite their important role in various processes, the structure and chaperone mechanism of sHsps remain poorly understood. We have accumulated extensive knowledge concerning the homododecameric plant Hsp18.1 and Hsp16.9 proteins, as well as their conditions for binding with porcine mitochondrial L-malate dehydrogenase (MDH) and firefly luciferase (Luc). The project presented here focuses on elucidating the structure of partially unfolded substrates when they are still in association with sHsps. The second part of this study involves characterization of the oligomeric state and subunit contacts of three sHsps.
机译：小型热休克蛋白（SHSP）和相关α-晶体是一类具有非常大的结合变性蛋白的低寡聚蛋白，从而防止在热应激时不可逆的蛋白质变性/聚集。在人类中，SHSP与肌肉疾病有关，某些癌症和神经变性疾病有关。尽管在各种过程中具有重要作用，但SHSP的结构和伴侣机制仍然明白很差。我们已经积累了关于同源聚氯胺植物HSP18.1和HSP16.9蛋白的广泛知识，以及它们与猪线粒体L-丙酸盐脱氢酶（MDH）和萤火虫荧光素酶（LUC）结合的条件。这里提出的该项目侧重于阐明当它们与SHSP相关联时部分展开的基板的结构。该研究的第二部分涉及三种SHSP的低聚状态和亚基接触的表征。

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