Yamaguchi, T.; Akao, K.; Koutsioubas, A.; Frielinghaus, H.; Kohzuma, T. Open-Bundle Structure as the Unfolding Intermediate of Cytochrome C′ Revealed by Small Angle Neutron Scattering. Biomolecules 2022, 12, 95, doi:10.3390/biom12010095.
Yamaguchi, T.; Akao, K.; Koutsioubas, A.; Frielinghaus, H.; Kohzuma, T. Open-Bundle Structure as the Unfolding Intermediate of Cytochrome C′ Revealed by Small Angle Neutron Scattering. Biomolecules 2022, 12, 95, doi:10.3390/biom12010095.
Yamaguchi, T.; Akao, K.; Koutsioubas, A.; Frielinghaus, H.; Kohzuma, T. Open-Bundle Structure as the Unfolding Intermediate of Cytochrome C′ Revealed by Small Angle Neutron Scattering. Biomolecules 2022, 12, 95, doi:10.3390/biom12010095.
Yamaguchi, T.; Akao, K.; Koutsioubas, A.; Frielinghaus, H.; Kohzuma, T. Open-Bundle Structure as the Unfolding Intermediate of Cytochrome C′ Revealed by Small Angle Neutron Scattering. Biomolecules 2022, 12, 95, doi:10.3390/biom12010095.
Abstract
The open-bundle structure of cytochrome c’ as an unfolding intermediate was determined by small-angle neutron scattering experiment (SANS). The four-α-helix bundle structure of Cyt c’ at neutral pH was transited to an open-bundle structure (at pD ~13), which is a joint-clubs 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 transitioned to a remarkably larger “open-bundle” structure at pD ~13 (Rg = 25 Å for the Cyt c’ monomer). Cyt c’ adopts an unstructured random coil structure at pD = 1.7 (Rg = 25 Å for the Cyt c’ monomer). Numerical partial scattering function analysis (joint-clubs) and ab initio modelling gave structures similar to the “open-bundle”, which retains the α-helices but loses the bundle structure.
Biology and Life Sciences, Biochemistry and Molecular Biology
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