Chain shuffling to modify properties of recombinant immunoglobulins.
(2002) In Methods in Molecular Biology 178. p.303-316- Abstract
- Combinatorial libraries and selection of variants from such libraries have proven to be a successful approach for identifying molecules with novel or improved properties. The importance of antibody (Ab) molecules in basic and applied research, as well as the extensive knowledge of how they interact with their antigen (Ag) targets, have made them favorite targets for modification by this approach. The binding site of Abs can be described as a set of modules that together make up the Ag-binding site. These modules may be defined either as the heavy-chain (HC) and light-chain (LC) variable domains (VH and VL respectively) or as the six individual complementarity-determining regions (CDRs) or hypervariable loops, which act together to form... (More)
- Combinatorial libraries and selection of variants from such libraries have proven to be a successful approach for identifying molecules with novel or improved properties. The importance of antibody (Ab) molecules in basic and applied research, as well as the extensive knowledge of how they interact with their antigen (Ag) targets, have made them favorite targets for modification by this approach. The binding site of Abs can be described as a set of modules that together make up the Ag-binding site. These modules may be defined either as the heavy-chain (HC) and light-chain (LC) variable domains (VH and VL respectively) or as the six individual complementarity-determining regions (CDRs) or hypervariable loops, which act together to form this structure. The variable CDRs reside in a relatively fixed framework region (FR) that makes up the basic structure and fold of the protein. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/107772
- author
- Lantto, Johan LU ; Jirholt, Pernilla ; Barrios del Pino, Yvelise LU and Ohlin, Mats LU
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Methods in Molecular Biology
- volume
- 178
- pages
- 303 - 316
- publisher
- Springer
- external identifiers
-
- scopus:0036358452
- ISSN
- 1940-6029
- DOI
- 10.1385/1-59259-240-6:303
- language
- English
- LU publication?
- yes
- id
- 1c7a288d-ba5c-4d09-894d-edca033e50a5 (old id 107772)
- alternative location
- http://www.springerlink.com/content/r62l820756072688/fulltext.pdf
- date added to LUP
- 2016-04-04 07:13:05
- date last changed
- 2022-02-28 03:24:37
@article{1c7a288d-ba5c-4d09-894d-edca033e50a5, abstract = {{Combinatorial libraries and selection of variants from such libraries have proven to be a successful approach for identifying molecules with novel or improved properties. The importance of antibody (Ab) molecules in basic and applied research, as well as the extensive knowledge of how they interact with their antigen (Ag) targets, have made them favorite targets for modification by this approach. The binding site of Abs can be described as a set of modules that together make up the Ag-binding site. These modules may be defined either as the heavy-chain (HC) and light-chain (LC) variable domains (VH and VL respectively) or as the six individual complementarity-determining regions (CDRs) or hypervariable loops, which act together to form this structure. The variable CDRs reside in a relatively fixed framework region (FR) that makes up the basic structure and fold of the protein.}}, author = {{Lantto, Johan and Jirholt, Pernilla and Barrios del Pino, Yvelise and Ohlin, Mats}}, issn = {{1940-6029}}, language = {{eng}}, pages = {{303--316}}, publisher = {{Springer}}, series = {{Methods in Molecular Biology}}, title = {{Chain shuffling to modify properties of recombinant immunoglobulins.}}, url = {{http://dx.doi.org/10.1385/1-59259-240-6:303}}, doi = {{10.1385/1-59259-240-6:303}}, volume = {{178}}, year = {{2002}}, }