%0 Journal Article
%A Yamaguchi, Takahide
%A Akao, Kouhei
%A Koutsioubas, Alexandros
%A Frielinghaus, Henrich
%A Kohzuma, Takamitsu
%T Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering
%J Biomolecules
%V 12
%N 1
%@ 2218-273X
%C Basel
%I MDPI
%M FZJ-2022-00285
%P 95 -
%D 2022
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ 35053243
%U <Go to ISI:>//WOS:000759795700001
%R 10.3390/biom12010095
%U https://juser.fz-juelich.de/record/904971