博碩士論文 92222040 完整後設資料紀錄

DC 欄位	值	語言
DC.contributor	物理學系	zh_TW
DC.creator	林政達	zh_TW
DC.creator	Cheng-ta Lin	en_US
dc.date.accessioned	2007-7-22T07:39:07Z
dc.date.available	2007-7-22T07:39:07Z
dc.date.issued	2007
dc.identifier.uri	http://ir.lib.ncu.edu.tw:444/thesis/view_etd.asp?URN=92222040
dc.contributor.department	物理學系	zh_TW
DC.description	國立中央大學	zh_TW
DC.description	National Central University	en_US
dc.description.abstract	本文研究蜂毒蛋白(melittin)與飽和鏈脂膜之作用。利用circular dichroism (CD)與isothermal titration calorimetry (ITC)測量蜂毒蛋白吸附飽和鏈脂膜的自由能，焓及熵，以熱力學探討吸附過程。 實驗結果顯示蜂毒蛋白吸附飽和鏈脂膜，與吸附未飽和鏈脂膜相同，皆為放熱反應，可知吸附為一個焓主導的過程，但吸附飽和鏈脂膜有異常放熱，推測蜂毒蛋白在飽和鏈脂膜上有聚集，這結果和文獻中利用螢光能量轉移技術(fluorescence energy transfer)的實驗相符。	zh_TW
dc.description.abstract	This thesis is to study the binding of melittin to saturated lipid membrane. We use circular dichroism (CD) and isothermal titration calorimetry (ITC) to measure the binding free energy, the binding enthalpy and the binding entropy for understanding the thermodynamics of binding process. The result reveals that, as the same as to the unsaturated lipid membrane, the melittin binding to the saturated lipid membrane is an exothermic reaction, indicating an enthalpy -driving process. However, there is an abnormal heat release for melittin binding to saturated lipid membrane, implying that melittin peptides are aggregated on membrane surface. This result is agreed with the measurement using fluorescence energy transfer technique.	en_US
DC.subject	微量測焓儀	zh_TW
DC.subject	人造脂膜	zh_TW
DC.subject	微胞	zh_TW
DC.subject	抗菌蛋白	zh_TW
DC.subject	旋二色光譜儀	zh_TW
DC.subject	Isothermal Titration Calorimetry	en_US
DC.subject	Circular Dichroism	en_US
DC.subject	viscle	en_US
DC.subject	DMPC	en_US
DC.subject	melittin	en_US
DC.title	蜂毒蛋白吸附飽和鏈脂膜的異常放熱	zh_TW
dc.language.iso	zh-TW	zh-TW
DC.title	Abnomal heat release of melittin binding to saturated lipid membrane	en_US
DC.type	博碩士論文	zh_TW
DC.type	thesis	en_US
DC.publisher	National Central University	en_US