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024 7 _ |a 10.3390/biom12010095
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100 1 _ |a Yamaguchi, Takahide
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245 _ _ |a Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering
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520 _ _ |a The dynamic structure changes, including the unfolding, dimerization, and transition from the compact to the open-bundle unfolding intermediate structure of Cyt c', were detected by a small-angle neutron scattering experiment (SANS). The structure of Cyt c' was changed into an unstructured random coil at pD = 1.7 (Rg = 25 Å for the Cyt c' monomer). The four-α-helix bundle structure of Cyt c' at neutral pH was transitioned to an open-bundle structure (at pD ~13), which is given by a numerical partial scattering function analysis as a joint-clubs model consisting of four clubs (α-helices) connected by short loops. The compactly folded structure of Cyt c' (radius of gyration, Rg = 18 Å for the Cyt c' dimer) at neutral or mildly alkaline pD transited to a remarkably larger open-bundle structure at pD ~13 (Rg = 25 Å for the Cyt c' monomer). The open-bundle structure was also supported by ab initio modeling.
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693 _ _ |a Forschungs-Neutronenquelle Heinz Maier-Leibnitz
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700 1 _ |a Akao, Kouhei
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700 1 _ |a Koutsioubas, Alexandros
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700 1 _ |a Frielinghaus, Henrich
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700 1 _ |a Kohzuma, Takamitsu
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773 _ _ |a 10.3390/biom12010095
|g Vol. 12, no. 1, p. 95 -
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856 4 _ |u https://juser.fz-juelich.de/record/904971/files/186.pdf
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