|
|
[期刊论文][article]
|
|
Domain interactions stabilize the alternatively folded state of an antibody Fab fragment
|
|
作 者：
|
Hauke Lilie;Johannes Buchner;
|
|
|
出版年：1995
|
|
页 码：43 - 46
|
|
出版社：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 .
|
关键字：
|
|
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
|
|
|
|
|
|
|
|
|
所属期刊
|
|
|
|
|
|
ISSN: 0014-5793
|
|
来自：John Wiley & Sons, Ltd.
|
|
