TY  - JOUR
A1  - Shou, Keyun
A1  - Bremer, Anne
A1  - Rindfleisch, Tobias
A1  - Knox-Brown, Patrick
A1  - Hirai, Mitsuhiro
A1  - Rekas, Agata
A1  - Garvey, Christopher J.
A1  - Hincha, Dirk K.
A1  - Stadler, Andreas M.
A1  - Thalhammer, Anja
T1  - Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity - an X-ray and light scattering study
JF  - Physical chemistry, chemical physics : a journal of European Chemical Societies
N2  - The plant stress protein COR15A stabilizes chloroplast membranes during freezing. COR15A is an intrinsically disordered protein (IDP) in aqueous solution, but acquires an alpha-helical structure during dehydration or the increase of solution osmolarity. We have used small- and wide-angle X-ray scattering (SAXS/WAXS) combined with static and dynamic light scattering (SLS/DLS) to investigate the structural and hydrodynamic properties of COR15A in response to increasing solution osmolarity. Coarse-grained ensemble modelling allowed a structure-based interpretation of the SAXS data. Our results demonstrate that COR15A behaves as a biomacromolecule with polymer-like properties which strongly depend on solution osmolarity. Biomacromolecular self-assembly occurring at high solvent osmolarity is initiated by the occurrence of two specific structural subpopulations of the COR15A monomer. The osmolarity dependent structural selection mechanism is an elegant way for conformational regulation and assembly of COR15A. It highlights the importance of the polymer-like properties of IDPs for their associated biological function.
Y1  - 2019
U6  - https://doi.org/10.1039/c9cp01768b
SN  - 1463-9076
SN  - 1463-9084
VL  - 21
IS  - 34
SP  - 18727
EP  - 18740
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  -