The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1
文献类型：期刊论文
| 作者 | Guo, ZY; Feng, YM |
| 刊名 | SCIENCE IN CHINA SERIES C-LIFE SCIENCES
 |
| 出版日期 | 2002 |
| 卷号 | 45期号:3页码:245-250 |
| 关键词 | insulin insulin-like growth factor 1 hybrid unfolding refolding |
| 通讯作者 | Feng, YM (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China., |
| 英文摘要 | Both Insulin and insulin-like growth factor 1 are members of insulin superfamily. They share homologous primary and tertiary structure as well as weakly overlapping biological activity. However, their folding behavior is different: insulin and its recombinant precursor (PIP) fold into one unique tertiary structure, while IGF-1 folds into two disulfides isomers with similar thermodynamic stability. To elucidate the molecular mechanism of their different folding behavior, we prepared a single-chain hybrid of insulin and IGF-1, [B10Glu]lnS/IGF-1(C), and studied its folding behavior compared with that of PIP and IGF-1. We also separated a major non-native disulfides isomer of the hybrid and studied its refolding. The data showed that the C-domain of IGF-1 did not affect the folding thermodynamics of insulin, that is, the primary structure of the hybrid encoded only one thermodynamically stable disulfides linkage. However, the folding kinetics of insulin was affected by the C-domain of IGF-1. |
| 学科主题 | Life Sciences & Biomedicine - Other Topics |
| 类目[WOS] | Biology |
| 关键词[WOS] | FACTOR-I ; FOLDING PATHWAY ; PROTEIN ; HYBRID |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000175701400003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2458]  |
| 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 | Guo, ZY,Feng, YM. The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1[J]. SCIENCE IN CHINA SERIES C-LIFE SCIENCES,2002,45(3):245-250. |
| APA | Guo, ZY,&Feng, YM.(2002).The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1.SCIENCE IN CHINA SERIES C-LIFE SCIENCES,45(3),245-250. |
| MLA | Guo, ZY,et al."The thermodynamic stability of insulin disulfides is not affected by the C-domain of insulin-like growth factor 1".SCIENCE IN CHINA SERIES C-LIFE SCIENCES 45.3(2002):245-250. |
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