König Nico, Paulus Michael, Julius Karin, Schulze Julian, Voetz Matthias, Tolan Metin
Fakultät Physik/DELTA, TU Dortmund, Dortmund 44221, Germany; Bayer AG, Leverkusen 51368, Germany.
Fakultät Physik/DELTA, TU Dortmund, Dortmund 44221, Germany.
Biophys Chem. 2017 Dec;231:45-49. doi: 10.1016/j.bpc.2017.05.016. Epub 2017 May 26.
In the present work two subclasses of the human antibody Immunoglobulin G (IgG) have been investigated by Small-Angle X-ray Scattering under high hydrostatic pressures up to 5kbar. It is shown that IgG adopts a symmetric T-shape in solution which differs significantly from available crystal structures. Moreover, high-pressure experiments verify the high stability of the IgG molecule. It is not unfolded by hydrostatic pressures of up to 5kbar but a slight increase of the radius of gyration was observed at elevated pressures.
在本研究中,通过小角X射线散射,在高达5千巴的高静水压力下对人类抗体免疫球蛋白G(IgG)的两个亚类进行了研究。结果表明,IgG在溶液中呈对称的T形,这与现有的晶体结构有显著差异。此外,高压实验证实了IgG分子的高稳定性。在高达5千巴的静水压力下它不会展开,但在高压下观察到回转半径略有增加。