教師資料查詢 | 類別: 期刊論文 | 教師: 李長欣 CHANG-SHIN LEE (瀏覽個人網頁)

標題:Dependence of Peptide Self-Association on Intermolecular Interaction by PFGNMR in TFE Aqueous Solution: C-terminal Analogues of NPY as Model Peptides
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
語言英文
ISSN0929-8665;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
國別荷蘭
公開徵稿
出版型式紙本
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