期刊論文
學年 | 100 |
---|---|
學期 | 1 |
出版(發表)日期 | 2011-10-01 |
作品名稱 | Dependence of Peptide Self-Association on Intermolecular Interaction by PFGNMR in TFE Aqueous Solution: C-terminal Analogues of NPY as Model Peptides |
作品名稱(其他語言) | 以神經胜肽碳端類似物作為模式從能量及結構的觀點探討分子間的作用對蛋白質分子的寡聚或自組裝的影響 |
著者 | Lee, Chang-Shin; Lin, Chia-Hao; Hsieh, Wan-Lun; Chiao, Szu-Min |
單位 | 淡江大學化學學系 |
出版者 | Bussum: Bentham Science Publishers Ltd. |
著錄名稱、卷期、頁數 | Protein & Peptide Letters 18(10), pp.1065-1071 |
摘要 | We have investigated the dependence of peptide oligomerization on intermolecular interaction in terms of both energetic and structural effect by PFGNMR. Three peptides, NPY[20-36], Pro34-NPY[20-36] and NPY[21-31], which are related to human NPY, were synthesized as models in this work. In contrast to NPY[20-36], both Pro34-NPY[20-36] and NPY[21-31] were found with descendent affinity with TFE cluster and continuous dissociating with increased temperature. The observed results can be accounted by the entropic change with temperature and the varied hydrophobic interactions between species due to the differed structures of peptides from each other. The removal of helical secondary structure or residues from C-terminal region may increase the energetic difference between peptide-peptide self-associating and peptidesolvent binding. This increased energetic difference leads to larger dependence of association-dissociation equilibrium on temperature and entropic increase while dissociating. |
關鍵字 | Association state; hydrophobic interaction; intermolecular interaction; neuropeptide Y; pulsed field gradient NMR; salvation |
語言 | en |
ISSN | 0929-8665 1875-5305 |
期刊性質 | 國外 |
收錄於 | SCI |
產學合作 | |
通訊作者 | Lee, Chang-Shin |
審稿制度 | |
國別 | NLD |
公開徵稿 | |
出版型式 | 紙本 |
相關連結 |
機構典藏連結 ( http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/58254 ) |