Effects of macromolecular crowding on the structure of a protein complex: a small-angle scattering study of superoxide dismutase.
Effects of macromolecular crowding on the structure of a protein complex: a small-angle scattering study of superoxide dismutase.
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DOI:
10.1016/j.bpj.2014.12.046
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发表时间:
2015-02-17
影响因子:
3.4
通讯作者:
Todd, Brian A.
中科院分区:
文献类型:
--
作者:
Rajapaksha, Ajith;Stanley, Christopher B.;Todd, Brian A.
Macromolecular crowding can alter the structure and function of biological macromolecules. We used small-angle scattering to measure the effects of macromolecular crowding on the size of a protein complex, SOD (superoxide dismutase). Crowding was induced using 400 MW PEG (polyethylene glycol),TEG (triethylene glycol), α-MG (methyl-α-glucoside), and TMAO (trimethylamine n-oxide). Parallel small-angle neutron scattering and small-angle x-ray scattering allowed us to unambiguously attribute apparent changes in radius of gyration to changes in the structure of SOD. For a 40% PEG solution, we find that the volume of SOD was reduced by 9%. Considering the osmotic pressure due to PEG, this deformation corresponds to a highly compressible structure. Small-angle x-ray scattering done in the presence of TEG suggests that for further deformation—beyond a 9% decrease in volume—the resistance to deformation may increase dramatically.
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