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

Abstract:

:The structure of the Fab fragment of the monoclonal antibody MAK 33 (kappa/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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Lilie H,Buchner J

doi

10.1016/0014-5793(95)00203-l

subject

Has Abstract

pub_date

1995-03-27 00:00:00

pages

43-6

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)00203-L

journal_volume

362

pub_type

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