title: Analysis of the extent of unfolding of denatured insulin-like growth factor.
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.
authors.affiliation: Institute of Molecular Medicine, The University of Texas, Houston 77030, USA. rchang@imm2.imm.uth.tmc.edu
authors.forename: J Y
authors.initials: JY
authors.lastname: Chang
authors.forename: W
authors.initials: W
authors.lastname: Märki
authors.forename: P H
authors.initials: PH
authors.lastname: Lai
mesh_terms: D019791:Guanidine / Q000737:chemistry; D006146:Guanidines / Q000737:chemistry; D011489:Protein Denaturation; D013002:Somatomedins / Q000737:chemistry*; D013861:Thiocyanates / Q000737:chemistry; D014508:Urea / Q000737:chemistry
chemical_list: D006146:Guanidines; D013002:Somatomedins; D013861:Thiocyanates; C054436:guanidine thiocyanate; D014508:Urea; D019791:Guanidine