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Analysis of the extent of unfolding of denatured insulin‐like growth factor
Author(s) -
Chang JuiYoa,
Lai PorHsiung
Publication year - 1999
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.8.7.1463
Subject(s) - disulfide bond , chemistry , yield (engineering) , thiol , crystallography , insulin like growth factor , growth factor , biochemistry , materials science , receptor , metallurgy
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.