Study of protein-protein interactions by fluorescence of tryptophan analogs: Application to immunoglobulin G binding domain of streptococcal protein G
文献类型:期刊论文
作者 | Li, Q; Du, HN; Hu, HY |
刊名 | BIOPOLYMERS
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出版日期 | 2003 |
卷号 | 72期号:2页码:116-122 |
关键词 | tryptophan analogs immunoglobulin G binding domain protein-protein interaction biosynthetic labeling fluorescence |
通讯作者 | Hu, HY (reprint author), Chinese Acad Sci, Key Lab Prote, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China., |
英文摘要 | The protein-protein interaction system often contains many fluorophores that may significantly interfere with the quantitative determination of the binding abilities. To solve this perplexing problem, we biosynthetically incorporated the two tryptophan analogs, 5-hydroxytryptophan and 7-azatryptophan, into the immunoglobulin G (IgG) binding domain of streptococcal protein G (PGBD). The exclusive excitation and novel fluorescence changes in both the intensity and anisotropy are beneficial to reporting the details of the interactions between PGBD and the IgG fragments and enable assessment of the binding abilities. The dissociation constants are estimated to be 0.28 muM for the binding of human Fc and 8.0 muM for mouse Fc. The results clearly demonstrate that labeling of tryptophan analogs has very little effect on the binding abilities and is broadly applicable to quantitatively studying protein-protein interactions in a whole biomolecular complex. (C) 2003 Wiley Periodicals, Inc. |
学科主题 | Biochemistry & Molecular Biology; Biophysics |
类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
关键词[WOS] | FC FRAGMENT ; FAB FRAGMENT ; 5-HYDROXYTRYPTOPHAN ; PROBE ; SPECTROSCOPY ; 7-AZATRYPTOPHAN ; ENHANCEMENT ; SURFACE ; NMR ; IGG |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000181362900005 |
版本 | 出版稿 |
源URL | [http://202.127.25.143/handle/331003/2258] ![]() |
专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
推荐引用方式 GB/T 7714 | Li, Q,Du, HN,Hu, HY. Study of protein-protein interactions by fluorescence of tryptophan analogs: Application to immunoglobulin G binding domain of streptococcal protein G[J]. BIOPOLYMERS,2003,72(2):116-122. |
APA | Li, Q,Du, HN,&Hu, HY.(2003).Study of protein-protein interactions by fluorescence of tryptophan analogs: Application to immunoglobulin G binding domain of streptococcal protein G.BIOPOLYMERS,72(2),116-122. |
MLA | Li, Q,et al."Study of protein-protein interactions by fluorescence of tryptophan analogs: Application to immunoglobulin G binding domain of streptococcal protein G".BIOPOLYMERS 72.2(2003):116-122. |
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