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Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c’ Revealed by Small Angle Neutron Scattering

Version 1 : Received: 30 May 2021 / Approved: 31 May 2021 / Online: 31 May 2021 (10:59:40 CEST)

How to cite: 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. Preprints 2021, 2021050739. https://doi.org/10.20944/preprints202105.0739.v1 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. Preprints 2021, 2021050739. https://doi.org/10.20944/preprints202105.0739.v1

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.

Keywords

Protein Unfolding 2; Cytochrome c’ 3; Small-Angle Neutron Scattering 4; Open-bundle structure

Subject

Biology and Life Sciences, Biochemistry and Molecular Biology

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