STRUCTURE DETERMINATION OF E COLI HSP 33, REDOX SENSITIVE CHAPERONIN

Hsp33是一种新的高度保守的热休克蛋白 大肠杆菌中的一家人。Jakob博士在Dr。 巴德威尔的实验室显示，HSP33是一种非常有效的 分子伴侣在保护未折叠蛋白质不可逆中的作用 聚合。根据环境的氧化还原状态，HSP33的S 监护人活动处于打开或关闭状态。在正态还原下 条件下，Hsp33处于非激活状态；然而，Hsp33变为激活状态 当暴露在氧化应激下时，折叠辅助蛋白。这是一个 已知由人类吞噬细胞诱导的压力，第一行 在体内实验中杀死入侵生物的防御支持我们的 体外研究结果表明，Hsp33是一种重要的 保护原核生物免受氧化应激。我们感兴趣的是 发现这种新型氧化还原敏感剂的结构机理 Hsp33的伴侣功能。BioCARS站上的数据采集 14-BM-C

Hsp33 is a member of a new and highly conserved heat shock protein family in E. coli. In vitro experiments by Dr. Jakob in Dr. Bardwell's laboratory reveal that Hsp33 is an extremely efficient molecular chaperone in protecting unfolding proteins from irreversible aggregation. Depending on the redox state of the environment, Hsp33's chaperone activity is either on or off. Under norinal reducing conditions, Hsp33 is inactive; however, Hsp33 turns into an active folding helper protein when exposed to oxidative stress. This is a stress known to be induced by human phagocytes, the first line of defense in killing invading organisms In vivo experiments support our in vitro findings by revealing that Hsp33 is an important player in protecting prokaryotes from oxidative stress. We are interested in finding the structural mechanism of this novel redox sensitive chaperone function of HSP33. Data collection on BioCARS Station 14-BM-C.