DOI: 10.1002/jmr.300070102. Kinetic analysis of engineered antibody‐antigen interactions

Kinetic analysis of engineered antibody‐antigen interactions

10.1002/jmr.300070102

Crossref journal-article

Wiley

Journal of Molecular Recognition (311)

Abstract

AbstractMolecular engineering antibodies has made it possible to produce specific domains of the antibody molecule and combine them with other protein domains to achieve new properties. Using site directed mutagenesis, amino acid residues can be exchanged within the binding site; and, by analysis of crystal structures, the positions of these amino acids can be determined in three dimensions at atomic resolution. In addition, gene libraries and phage selection technology can be used to generate new antibody fragments directly from a gene pool. Both mutagenesis and selection from libraries offer opportunities to identify antibody‐derived molecules with altered and useful antigen recognition properties. The detailed analysis both kinetic and equilibrium binding affinity are therefore essential to understand the activity of the molecules resulting from antibody engineering and to guide the progress of their further design. The paper reviews recently evolving techniques for the binging analysis of antibodies, their functional domains and antibody chimerae.

Bibliography

Malmqvist, M. (1994). Kinetic analysis of engineered antibodyâantigen interactions. Journal of Molecular Recognition, 7(1), 1â7. Portico.

Authors 1

Magnus Malmqvist (first)

References 57 Referenced 13

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Dates

Type	When
Created	20 years, 3 months ago (May 29, 2005, 6:33 a.m.)
Deposited	1 year, 10 months ago (Oct. 23, 2023, 7:59 p.m.)
Indexed	1 year, 7 months ago (Jan. 15, 2024, 1:22 p.m.)
Issued	31 years, 6 months ago (March 1, 1994)
Published	31 years, 6 months ago (March 1, 1994)
Published Online	21 years, 7 months ago (Feb. 3, 2004)
Published Print	31 years, 6 months ago (March 1, 1994)

Funders 0

None

BibTeX

@article{Malmqvist_1994, title={Kinetic analysis of engineered antibody‐antigen interactions}, volume={7}, ISSN={1099-1352}, url={http://dx.doi.org/10.1002/jmr.300070102}, DOI={10.1002/jmr.300070102}, number={1}, journal={Journal of Molecular Recognition}, publisher={Wiley}, author={Malmqvist, Magnus}, year={1994}, month=mar, pages={1–7} }

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