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Characterization of the linker peptide of the single‐chain F v fragment of an antibody by NMR spectroscopy
Author(s) -
Freund Christian,
Ross Alfred,
Guth Birgith,
Plückthun Andreas,
Holak Tad A.
Publication year - 1993
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(93)80070-b
Subject(s) - linker , chemistry , peptide , nuclear magnetic resonance spectroscopy , stereochemistry , fragment (logic) , folding (dsp implementation) , glycine , crystallography , amino acid , biochemistry , computer science , electrical engineering , programming language , engineering , operating system
A comparison of the single‐chain F v fragment of the antibody McPC603 (scF v ) with its corresponding unlinked F v . fragment has been carried out with 15 N‐edited NMR spectroscopy. The two F v , fragments adopt the same structure, indicating that the linker does not perturb the folding of the domains. This also directly demonstrates that folding in vivo (F v fragment) and in vitro (scF v . fragment) leads to the same structure. The main differences in the spectra of the uniformly 15 N‐labeled scF v and F v fragments are due to signals of Gly and Ser from the linker peptide of the scF v , fragment. The linker peptide has been mapped with NMR spectra of 15 N‐glycine‐ and 15 N‐glycine 15 N‐serine‐labeled scF v fragments. The 15 N T 2 , relaxation data indicate that the linker peptide is more flexible than the rest of the molecule.