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Chain shuffling to modify properties of recombinant immunoglobulins.

Lantto, Johan LU ; Jirholt, Pernilla; Barrios del Pino, Yvelise LU and Ohlin, Mats LU (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:
author
organization
publishing date
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
2007-07-09 09:41:54
date last changed
2017-08-20 04:35:54
@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},
  volume       = {178},
  year         = {2002},
}