Peptide models of four possible insulin folding intermediates with two disulfides
文献类型：期刊论文
| 作者 | Jia, XY; Guo, ZY; Wang, Y; Xu, Y; Duan, SS; Feng, YM |
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2003 |
| 卷号 | 12期号:11页码:2412-2419 |
| 关键词 | insulin folding intermediate disulfide bonds kinetics |
| 通讯作者 | Feng, YM (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Key Lab Proteom, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China., |
| 英文摘要 | The single-chain insulin (PIP) can spontaneously fold into native structure through preferred kinetic intermediates. During refolding, pairing of the first disulfide A20-B19 is highly specific, whereas pairing of the second disulfide is likely random because two two-disulfide intermediates have been trapped. To get more details of pairing property of the second disulfide, four model peptides of possible folding intermediates with two disulfides were prepared by protein engineering, and their properties were analyzed. The four model peptides were named [A20-B19, A7-B7]PIP, [A20-B19, A6-B7]PIP, [A20-B19, A6-A11]PIP, and [A20-B19, A7-A11]PIP according to their remaining disulfides. The four model peptides all adopt partially folded structure with moderate conformational differences. In redox buffer, the disulfides of the model peptides are more easily reduced than those of the wild-type PIP. During in vitro refolding, the reduced model peptides share similar relative folding rates but different folding yields: The refolding efficiency of the reduced [A20-B19, A7-A11]PIP is about threefold lower than that of the other three peptides. The present results indicate that the folding intermediates corresponding to the present model peptides all adopt partially folded conformation, and can be formed during PIP refolding, but the chance of forming the intermediate with disulfide [A20-B19, A7-A11] is much lower than that of forming the other three intermediates. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | GROWTH-FACTOR-I ; MASS-SPECTROMETRY ; BINDING-PROTEIN ; IGF-I ; PATHWAY ; DESIGN ; ANALOG ; BONDS ; CYANYLATION ; PRECURSOR |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000186333800003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2361]  |
| 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 | Jia, XY,Guo, ZY,Wang, Y,et al. Peptide models of four possible insulin folding intermediates with two disulfides[J]. PROTEIN SCIENCE,2003,12(11):2412-2419. |
| APA | Jia, XY,Guo, ZY,Wang, Y,Xu, Y,Duan, SS,&Feng, YM.(2003).Peptide models of four possible insulin folding intermediates with two disulfides.PROTEIN SCIENCE,12(11),2412-2419. |
| MLA | Jia, XY,et al."Peptide models of four possible insulin folding intermediates with two disulfides".PROTEIN SCIENCE 12.11(2003):2412-2419. |
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