中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin

文献类型:期刊论文

作者Guo, ZY; Wang, S; Tang, YH; Feng, YM
刊名BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
出版日期2004
卷号1699期号:1页码:103-109
关键词insulin foldability secretion refolding stability
通讯作者Feng, YM (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Key Lab Proteom, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,fengym@sunm.shcnc.ac.cn
英文摘要Natural polypeptide chain usually can spontaneously fold into tightly compact native structure. This capability is the so-called foldability. However, how the foldability is encoded in the polypeptide chain is still poorly understood. The structure of insulin has been well solved and extensively investigated. Therefore, insulin provides a good model for investigating the role of individual residue to the sequence foldability. In insulins from different species there are three highly conserved Val residues (A3Val, B12Val, and B18Val), but their contribution to the insulin foldability is still unknown. Here, a single-chain insulin (PIP) was used to investigate the contribution of the three conserved valine residues to the foldability. Five PIP mutants, [A3S]PIP, [A3T]PIP, [B12A]PIP, [B18T]PIP, and [B18L]PIP, were used in the studies, and their structural changes, secretion efficiency, structural stability, disulfide stability, and in vitro refolding efficiency were analyzed. The effects of the mutations on the PIP foldability are multifold: as a whole, mutation of A3Val has only moderate effect; while mutation of B12Val has significant detriment; hydrophobic replacement of B18Val is more tolerant than hydrophilic substitution as foldability is concerned. Therefore, the three highly conserved valine residues have different contributions to the insulin foldability, and their contribution might be ranked as B12Val>B18Val>A3Val. (C) 2004 Elsevier B.V. All rights reserved.
学科主题Biochemistry & Molecular Biology; Biophysics
类目[WOS]Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]RECEPTOR-BINDING ; MUTATIONAL ANALYSIS ; MOLECULE ; MONOMER ; PATHWAY ; SURFACE ; DESIGN ; CHAINS ; ANALOG
收录类别SCI
语种英语
WOS记录号WOS:000221807800009
版本出版稿
源URL[http://202.127.25.143/handle/331003/2195]  
专题上海生化细胞研究所_上海生科院生化细胞研究所
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GB/T 7714
Guo, ZY,Wang, S,Tang, YH,et al. Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2004,1699(1):103-109.
APA Guo, ZY,Wang, S,Tang, YH,&Feng, YM.(2004).Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1699(1),103-109.
MLA Guo, ZY,et al."Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1699.1(2004):103-109.

入库方式: OAI收割

来源:上海生物化学与细胞生物学研究所

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