第一部分主要是以蛋白質質譜的分析方法去討論寒冷效應會如何影響稻米芽鞘，並且觀察當低溫逆境施加在水稻上時會產生何種變化，並進一步探討其原因。
我們將前處理過後的稻米芽鞘水溶性蛋白質，以二維電泳分析技術搭配質譜儀的(LC/MS)分析，對稻米芽鞘的蛋白質作分析，觀察寒冷效應(chilling effect)會如何影響稻米芽鞘中的蛋白質，並探討其中產生差異的原因。
並從二維膠體電泳分析結果發現經歷過低溫環境的稻米芽鞘之蛋白質，在分子量15kDa有出現一個新的蛋白質點，我們將此變異的蛋白質點，利用質譜儀進一步的進行分析，並執行蛋白質鑑定。
第二部分我們主要是利用稻米芽鞘胰蛋白酶抑制劑(RCTI)的domain I，由於結構的因素，過去的研究指出環狀之蛋白酶抑制劑效果比起線性來說較為優異，故我們將domain I部分之序列改造成環狀的結構，並利用酵素動力學方法去測試其抑制活性以及分析為何種抑制作用類型，雖然抑制劑的效果沒有我們預計中如此理想，但實驗的結果還是指出模擬環狀之胰蛋白酶抑制劑的確具有抑制效果，而得到的Ki為12.07*10-7M。
關鍵字:低溫逆境、二維膠體電泳分析、質譜分析、稻米芽鞘胰蛋白酶抑制劑、模擬肽學、酵素動力學

Part I showed that the chilling effect on the protein of rice coleoptiles with proteomic method. The overall proteins extracted from the rice coleoptiles at the 4 oC were compared with those grown at room temperature through 2D gel electrophoresis. The proteins were analysed after purification. 2D gel electrophoresis was employed to investigate the differences between experimental and control ones. One additional protein spot were observed with molecular weight around 13kDa for the coleoptiles grown at 4 oC. Furthermore, the protein spots were identified with LC/MSMS, then identified showed an uncharacterized protein which acc number is A2Z6D8_ORYSI.
Part II described the use of domain I of rice coleoptile protease inhibitor from rice seedlings grown in hypoxia condition as scaffold, a cyclic 33-mer peptide with7-33 disulfide-cyclized peptides . The study of its activity and changes in detail of secondary structure upon complexation of inhibitors with trypsin enzyme were reported. The cyclic peptide inhibitor and disulfide-cyclic peptide inhibitor exhibited inhibition towards trypsin enzyme. The inhibition constants obtained for cyclic inhibitors were 12.3x 10-7M.
Key words: chilling effect、2D gel electrophoresis、LC/MS、protein identification、cyclic peptide inhibitor、inhibition constants

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