Analysis of the extent of unfolding of denatured insulin-like growth factor

被引：16

作者：

Chang, JY

Märki, W

Lai, PH

机构：

[1] Univ Texas, Inst Mol Med, Res Ctr Prot Chem, Houston, TX 77030 USA

[2] Novartis AG, Pharmaceut Res Labs, Basel, Switzerland

[3] Prot Inst Inc, Broomall, PA 19008 USA

来源：

PROTEIN SCIENCE | 1999年 / 8卷 / 07期

关键词：

denaturation; GdmCl; GdmSCN; insulin-like growth factor; protein folding; scrambled proteins; unfolding; unfolding intermediates; urea;

D O I：

10.1110/ps.8.7.1463

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Insulin-like growth factor (IGF-1) contains three disulfide bonds. In the presence of denaturant and thiol catalyst, IGF-1 shuffles its native disulfide bends and denatures to form a mixture of scrambled isomers. The composition of scrambled IGF varies under different denaturing conditions. Among the 14 possible scrambled IGF isomers, the yield of the beads-form isomer is shown to be directly proportional to the strength of the denaturing condition. This paper demonstrates a new approach to quantify the extent of unfolding of the denatured protein.

引用

收藏

页码：1463 / 1468

页数：6

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