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Domain interactions stabilize the alternatively folded state of an antibody Fab fragment
Author(s) -
Lilie Hauke,
Buchner Johannes
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00203-l
Subject(s) - chemistry , immunoglobulin light chain , covalent bond , fragment (logic) , disulfide bond , stereochemistry , disulfide linkage , immunoglobulin fab fragments , crystallography , antibody , peptide sequence , biochemistry , enzyme , organic chemistry , cysteine , computer science , immunology , biology , programming language , gene , complementarity determining region
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 .