Domain interactions stabilize the alternatively folded state of an antibody Fab fragment

FEBS Letters

Lilie, Hauke¹  Buchner, Johannes¹ 

[1] Institut für Biophysik und Biophysikalische Chemie, Universität Regensburg, 93040 Regensburg, Germany

关键词: Denaturation;    Molten globule;    Tertiary structure;    Fab fragment;    Fabalk;    Fab fragment with the interchain disulfide reduced and alkylated;    DTT;    dithiothreitol;    CD;    circular dichroism;    gdm/Cl;    guanidinium hydrochloride;    FKBP;    FK506 binding protein;    Fd;    proteolytically derived fragment of the heavy chain;    containing the two N-terminal domains;   

DOI  :  10.1016/0014-5793(95)00203-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of the Fab fragment of the monoclonal antibody MAK 33 (κ/IgG1) at pH 2 was characterized. Spectroscopic and kinetic analysis revealed a molten globule-like state, characterized by elements of secondary structure but less defined tertiary contacts than in the native state. However, some aromatic side chains are in an asymmetrical environment. This structure was not detected using the isolated light chain or a Fab fragment lacking the covalent linkage of the light chain and Fd via the C-terminal disulfide bond. Therefore, interactions between the two chains, stabilized by the interchain disulfide within the Fab fragment, are essential for formation of the alternatively folded state.

【 授权许可】

Unknown