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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
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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

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