Antibodies under pressure: A Small-Angle X-ray Scattering study of Immunoglobulin G under high hydrostatic pressure

被引：10

作者：

Koenig, Nico ^{[1
,2
,3
,4
]}

Paulus, Michael ^{[1
]}

Julius, Karin ^{[1
]}

Schulze, Julian ^{[1
]}

Voetz, Matthias ^{[2
]}

Tolan, Metin ^{[1
]}

机构：

[1] TU Dortmund, Falc Phys, DELTA, D-44221 Dortmund, Germany

[2] Bayer AG, D-51368 Leverkusen, Germany

[3] Forschungszentrum Julich, JCNS, D-52425 Julich, Germany

[4] Forschungszentrum Julich, ICS, D-52425 Julich, Germany

来源：

BIOPHYSICAL CHEMISTRY | 2017年 / 231卷

关键词：

Small-Angle X-ray Scattering (SAXS); High hydrostatic pressure (HHP); Immunoglobulin G (IgG) antibody; Stability; Solution conformation; PROTEIN CRYSTALLIZATION; MONOCLONAL-ANTIBODIES; IGG SUBCLASSES; CRYSTAL; MACROMOLECULES; SAXS;

D O I：

10.1016/j.bpc.2017.05.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 5 kbar. 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 5 kbar but a slight increase of the radius of gyration was observed at elevated pressures.

引用

页码：45 / 49

页数：5

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