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分子伴侣与蛋白质折叠
引用本文:井明艳,孙建义.分子伴侣与蛋白质折叠[J].科技通报,2004,20(5):407-411.
作者姓名:井明艳  孙建义
作者单位:浙江大学,动物分子营养学教育部重点实验室,杭州,310029
摘    要:新合成的多肽链必须先经折叠和装配后形成特定的三维结构才具有活性.在多肽链折叠过程中,往往会产生折叠异常蛋白,形成集聚体.分子伴侣可有效地调控多肽链的正确折叠,从而避免集聚体的形成.文章主要对分子伴侣的定义、作用、种类、特性等做一介绍。

关 键 词:分子伴侣  热休克蛋白70s  陪伴蛋白
文章编号:1001-7119(2004)05-0407-05
修稿时间:2003年7月28日

Molecular Chaperones and Protein Folding
JING Ming-yan,SUN Jian-yi n,Zhejiang University,Hangzhou ,China.Molecular Chaperones and Protein Folding[J].Bulletin of Science and Technology,2004,20(5):407-411.
Authors:JING Ming-yan  SUN Jian-yi n  Zhejiang University  Hangzhou  China
Institution:JING Ming-yan,SUN Jian-yi n,Zhejiang University,Hangzhou 310029,China)
Abstract:Newly synthesized polypeptide chains must fold and assemble into unique three-dimensional structures in order to become functionally active. In the folding process,many misfolded proteins maybe produced and thus accumulate as aggregates. Maintaining quality control over polypeptide chains folding depends on molecular chaperones, which can prevent aggregation. This review summarizes the definition, roles, species, properties of chaperone and so on.
Keywords:Molecular chaperones  Hsp70s  chaperonins
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