Cloning, Expression, Purification and Chaperone-like Activity of a Small Heat-shock Protein, HSP16.1, from Caenorhabditis elegans
Date Issued
2004
Date
2004
Author(s)
Shih, Chung-Cheng
DOI
zh-TW
Abstract
Small heat shock proteins (sHSPs) form a diverse family of proteins that are produced under various stresses in all organisms. It has been shown that they have chaperone-like activity, which can bind unfolded or misfolded proteins and maintain them in a folding-competent state. The common structural features of small heat shock proteins comprise an N-terminal domain and a C-terminal tail, which flank the evolutionarily conserved
Subjects
線蟲
小熱休克蛋白
分子保護活性
分子保護者
small heat-shock protein,chpaerone-like activity
molecular chaperones
Type
other
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