Please wait a minute...

中国生物工程杂志

China Biotechnology
China Biotechnology  2006, Vol. 26 Issue (0): 157-161    DOI:
    
Molecular Chaperones and Protein Folding
Download: HTML   PDF(466KB) HTML
Export: BibTeX | EndNote (RIS)      

Abstract  

The newly-synthesized protein must fold into its proper three-dimensional structure to be useful to the cell, in many situations efficient folding of many newly synthesized proteins depends on assistance from molecular chaperones, which serve to prevent protein misfolding and degradation in the crowded environment of the cell. In this article, at first we discuss the concept and classification of molecular chaperones, next describe several new hypothesises about how protein folds, and lastly use Hsp70 and Hsp90 as examples introducing the latest research progress on the function of molecular chaperones in facilitating protein folding.



Key wordsMolecular Chaperones      Protein Folding      Hsp70      Hsp90     
Received: 13 March 2006      Published: 15 June 2006
Cite this article:

. Molecular Chaperones and Protein Folding. China Biotechnology, 2006, 26(0): 157-161.

URL:

https://manu60.magtech.com.cn/biotech/     OR     https://manu60.magtech.com.cn/biotech/Y2006/V26/I0/157

[1] HUANG Yu,HUANG Shu-ting,ZHANG Xi-mei,LIU Yan. Cloning and Functional Analysis of the Promoter of HSP70 Gene in Gobiocypris rarus[J]. China Biotechnology, 2019, 39(10): 9-16.
[2] . The progress of Chloramphenicol and tetracycline inhibit bacterial protein secretion[J]. China Biotechnology, 2010, 30(07): 0-0.
[3] . Prokaryotic Expression, Purification of human 14-kDa phosphohistidine phosphatase and its interacting protein study in vitro[J]. China Biotechnology, 2010, 30(07): 0-0.
[4] ZHENG Ji-Sheng, XU Gong-Bao, HOU Gong-Yan, ZHANG Xue-Hua, HOU Ji-Bei. Study on the Immune Efficiency for General Vaccine Against Avian Influenza Virus Using Human Mycobacterium Tuberculosis hsp70 as the Carrier for Peptide Epitopes[J]. China Biotechnology, 2009, 29(12): 24-29.