Study of binding interaction between Pif80 protein fragment and aragonite

NCU Institutional Repository > 理學院 > 化學學系 > 期刊論文 > Item 987654321/101844

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://ir.lib.ncu.edu.tw/handle/987654321/101844

题名:	Study of binding interaction between Pif80 protein fragment and aragonite
作者:	杜遠朋;Du, Yuan-Peng;Chang, Hsun-Hui;Yang, Sheng-Yu;Huang, Shing-Jong;Tsai, Yu-Ju;Huang, Joseph Jen-Tse;Chan, Jerry Chun Chung
贡献者:	理學院化學學系
关键词:	639/301/54/1754;639/301/930/878/1264;Amino acid sequence;Animals;Calcium Carbonate - chemistry;Calcium Carbonate - metabolism;Chitin;Crystallization;Extracellular Matrix Proteins - chemistry;Extracellular Matrix Proteins - metabolism;Humanities and Social Sciences;Mineralization;multidisciplinary;Nucleation;Peptide Fragments - chemistry;Peptide Fragments - metabolism;Peptides;Pinctada - metabolism;Protein Binding;Proteins;Science;Science (multidisciplinary)
日期:	2016-08-03
上传时间:	2026-04-21 14:47:50 (UTC+8)
出版者:	Nature Publishing Group;London: Nature Publishing Group UK
摘要:	摘要： Pif is a crucial protein for the formation of the nacreous layer in Pinctada fucata . Three non-acidic peptide fragments of the aragonite-binding domain (Pif80) are selected, which contain multiple copies of the repeat sequence DDRK, to study the interaction between non-acidic peptides and aragonite. The polypeptides DDRKDDRKGGK (Pif80-11) and DDRKDDRKGGKDDRKDDRKGGK (Pif80-22) have similar binding affinity to aragonite. Solid-state NMR data indicate that the backbones of Pif80-11 and Pif80-22 peptides bound on aragonite adopt a random-coil conformation. Pif80-11 is a lot more effective than Pif80-22 in promoting the nucleation of aragonite on the substrate of β-chitin. Our results suggest that the structural arrangement at a protein-mineral interface depends on the surface structure of the mineral substrate and the protein sequence. The side chains of the basic residues, which function as anchors to the aragonite surface, have uniform structures. The role of basic residues as anchors in protein-mineral interaction may play an important role in biomineralization. 其他題名： Sci Rep 出版者： London: Nature Publishing Group UK 出版日期： 2016-08-03 出處： Scientific reports, 2016-08, Vol.6 (1), p.30883-30883, Article 30883 資源來源： Publicly Available Content Database 版權： The Author(s) 2016 版權： Copyright Nature Publishing Group Aug 2016 版權： Copyright © 2016, The Author(s) 2016 The Author(s) 識別號： ISSN: 2045-2322 識別號： EISSN: 2045-2322 識別號： DOI: 10.1038/srep30883 識別號： PMID: 27484975
显示于类别:	[化學學系] 期刊論文

文件中的档案:

档案	描述	大小	格式	浏览次数
index.html		0Kb	HTML	23	检视/开启

在NCUIR中所有的数据项都受到原著作权保护.

社群 sharing

数据加载中.....