2014
DOI: 10.1021/bi500497s
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Formation of Domain-Swapped Oligomer of Cytochrome c from Its Molten Globule State Oligomer

Abstract: Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule state to neutral pH state under high protein and ion concentrations. The amount of oligomeric cyt c obtained depended on the nature of the anion (chaotropic or kosmotropic) in the solution: ClO4(-) (oligomers, 11% ± 2% (heme unit)), SCN(-) (10% ± 2%), I(-) (6% ± 2%)… Show more

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Cited by 24 publications
(24 citation statements)
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“…The lower curvature in the equine data yields ΔC p ‡ = 1.8 ± 0.9 kcal mol −1 K −1 , indicating that dimer dissociation requires significant, but possibly not complete, unfolding of the dimer subunits. Preparation of the equine Cyt c dimer in vitro requires refolding from a denatured 37,65 or molten globule state, 66 also consistent with the transition state for the monomer-dimer equilibrium being unfolded Cyt c . In a number of other instances, the transition state for the monomer-dimer equilibrium for domain-swapped dimers also appears to require full unfolding of the protein.…”
Section: Resultssupporting
confidence: 54%
“…The lower curvature in the equine data yields ΔC p ‡ = 1.8 ± 0.9 kcal mol −1 K −1 , indicating that dimer dissociation requires significant, but possibly not complete, unfolding of the dimer subunits. Preparation of the equine Cyt c dimer in vitro requires refolding from a denatured 37,65 or molten globule state, 66 also consistent with the transition state for the monomer-dimer equilibrium being unfolded Cyt c . In a number of other instances, the transition state for the monomer-dimer equilibrium for domain-swapped dimers also appears to require full unfolding of the protein.…”
Section: Resultssupporting
confidence: 54%
“…1) [4,5]. It has been reported that horse cyt c forms oligomers during protein folding [16,17], and more domain-swapped oligomers are formed for higher protein concentrations during folding of horse cyt c [16]. HT cyt c552 forms domain-swapped oligomers in Escherichia coli (E. coli) cells during expression, where the structure of the dimer formed in E. coli was similar to that of the dimer obtained by the ethanol treatment [18].…”
Section: Introductionmentioning
confidence: 87%
“…Refolding experiments of ribonuclease A [ 34 ] and molecular dynamics simulations of γ-crystallin [ 35 ] have revealed that these proteins form domain-swapped oligomers via the folding intermediates possessing regions with native-like structures. We have reported that horse cyt c forms domain-swapped oligomers by the interaction between the N- and C-terminal α-helices at the early stage of folding from its unfolded state [ 36 ], and the interaction important for formation of domain-swapped oligomers exists in the molten globule state [ 37 ]. The hinge loop, a segment of the polypeptide chain that links the swapped domain and the rest of the protein, plays an important role in stabilizing the domain-swapped conformation [ 4 ].…”
Section: Introductionmentioning
confidence: 99%