Hostname: page-component-cd9895bd7-p9bg8 Total loading time: 0 Render date: 2024-12-27T07:27:39.842Z Has data issue: false hasContentIssue false
  • English
  • Français

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

Published online by Cambridge University Press:  01 July 1999

JUI-YOA CHANG ,
WALTER MÄRKI  and
POR-HSIUNG LAI
JUI-YOA CHANG
Affiliation:
Research Center for Protein Chemistry, Institute of Molecular Medicine, The University of Texas, Houston, Texas 77030
WALTER MÄRKI
Affiliation:
Pharmaceuticals Research Laboratories, Novartis AG, Basel, Switzerland
POR-HSIUNG LAI
Affiliation:
The Protein Institute Inc., Broomall, Pennsylvania 19008
Get access

Abstract

Insulin-like growth factor (IGF-1) contains three disulfide bonds. In the presence of denaturant and thiol catalyst, IGF-1 shuffles its native disulfide bonds 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.

Keywords

denaturationGdmClGdmSCNinsulin-like growth factorprotein foldingscrambled proteinsunfoldingunfolding intermediatesurea
Type
Research Article
Information
Protein Science , Volume 8 , Issue 7 , July 1999 , pp. 1463 - 1468
Copyright
© 1999 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)