邱式鴻臺灣大學:生化科學研究所施駿成Shih, Chung-ChengChung-ChengShih2007-11-262018-07-062007-11-262018-07-062004http://ntur.lib.ntu.edu.tw//handle/246246/52787當生物體遭到不同逆境壓力刺激時,它們會產生一群小熱休克蛋白。已知小熱休克蛋白具有分子保護活性,可與錯誤摺疊蛋白結合並使它們維持在易摺疊狀態。小熱休克蛋白在結構上的特色是在中間有一段保守不變的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中文摘要 3 英文摘要 4 縮寫表 6 第一章 序論 7 第二章 材料及方法 17 第三章 實驗結果 35 第四章 討論與未來展望 41 第五章 圖表 46 第六章 參考文獻 788527620 bytesapplication/pdfen-US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 activitymolecular chaperones線蟲小熱休克蛋白HSP16.1的選殖、表現、純化及分子保護活性研究Cloning, Expression, Purification and Chaperone-like Activity of a Small Heat-shock Protein, HSP16.1, from Caenorhabditis elegansotherhttp://ntur.lib.ntu.edu.tw/bitstream/246246/52787/1/ntu-93-R91242020-1.pdf