
GroEL - Wikipedia
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. [5] It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES.
分子伴侣---蛋白质折叠的促进者 - 知乎 - 知乎专栏
2023年8月9日 · 细菌I组伴侣蛋白,称为GroEL/GroES。 在大肠杆菌中,GroEL被认为参与了大约10%的蛋白质的折叠。 II类伴侣蛋白存在于真核细胞的细胞质中(如哺乳动物)和古细菌中的TriC,每个环中可以有8到9个同质或异质亚基,“盖子”功能被整合到这些亚基本身中——不需要 ...
GroEL and the GroEL-GroES Complex - PubMed
In this article, an overview is presented on GroEL and the GroEL-GroES complex, with emphasis on their morphological variations, and some potential applications to the fabrication of nanocomposites using GroEL as a nano-block.
GroEL—A Versatile Chaperone for Engineering and a Plethora of ...
GroEL may be engineered for stabilization, biosynthesis, or soluble expression of polypeptides in any of its forms: as a full-sized oligomer, a monomer, or a separate apical domain, called a minichaperone. All these cases are described in detail below.
分子伴侣 - 百度百科
Cpns 又分为两组:GroEL(Hsp60) 家族和TriC 家族。 GroEL 型的 Cpns 存在于真细菌、 线粒体 和 叶绿体 中,由双层 7 个亚基组成的圆环组成,每个亚基分子量约为 60Ku。
Iterative annealing mechanism explains the functions of the GroEL …
GroEL, assembled from seven identical subunits, is a homo oligomer with two rings that are stacked back‐to‐back, which confers it in an unusual rare seven fold symmetry in the resting (T or taut) state.
Molecular chaperone GroEL/ES: unfolding and refolding processes
The representatives of the Escherichia coli chaperone system GroEL (Hsp60) and GroES (Hsp10) have been studied most intensively. GroEL consists of 14 identical subunits combined into two interacting ring-like structures of seven subunits each, while the co-chaperone GroES interacting with GroEL consists of seven identical subunits combined into ...
分子伴侣 - 维基百科,自由的百科全书
图1:细菌的GroES/GroEL分子伴侣复合体俯视图. 分子伴侣(英語: chaperone ,molecular chaperone) [1] [註 1] 又译侣伴蛋白、伴護蛋白、分子伴護蛋白 [3] ,是一类协助细胞内分子组装和协助蛋白质折叠的蛋白质。
GroEL: More than Just a Folding Cage - ScienceDirect
2006年6月2日 · The chaperonin GroEL has been thought of as an important but passive player in protein folding, providing an encapsulated environment that allows folding to proceed unimpaired by aggregation.
大肠杆菌分子效伴侣GroEL和GroES蛋白的高效表达、纯化与鉴定
This article concerns molecular chaperone GroEL (with its partner GroES protein), a member of heat shock protein 60 (hsp60) family in E.coli. The plasmid pGroESL contains groEL and groES genes of E.coli.