TY  - JOUR
AU  - Yamaguchi, Takahide
AU  - Akao, Kouhei
AU  - Koutsioubas, Alexandros
AU  - Frielinghaus, Henrich
AU  - Kohzuma, Takamitsu
TI  - Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering
JO  - Biomolecules
VL  - 12
IS  - 1
SN  - 2218-273X
CY  - Basel
PB  - MDPI
M1  - FZJ-2022-00285
SP  - 95 -
PY  - 2022
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 35053243
UR  - <Go to ISI:>//WOS:000759795700001
DO  - DOI:10.3390/biom12010095
UR  - https://juser.fz-juelich.de/record/904971
ER  -