dc.contributor.author |
Crampton, Michael C
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dc.contributor.author |
Berger, E
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dc.contributor.author |
Louw, ME
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dc.date.accessioned |
2008-12-12T12:24:13Z |
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dc.date.available |
2008-12-12T12:24:13Z |
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dc.date.issued |
2008-11 |
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dc.identifier.citation |
Crampton, M.C., Berger, E. and Louw, M.E. 2008. To 'display' or not to 'display'- that is the peptide. Science Real and Relevant: 2nd CSIR Biennial Conference, CSIR International Convention Centre Pretoria, 17 & 18 November 2008, pp 1 |
en |
dc.identifier.uri |
http://hdl.handle.net/10204/2741
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dc.description |
Science Real and Relevant: 2nd CSIR Biennial Conference, CSIR International Convention Centre Pretoria, 17 & 18 November 2008 |
en |
dc.description.abstract |
Microbial cell surface display is the anchoring of a heterologous protein or peptide (passenger) to the outside of the cell wall as a fusion to a cell surface associated protein (carrier). This technology has been used extensively for both eukaryotic and prokaryotic systems but has mainly focused around phages (Etz et al, 2001), yeast (Kondo and Ueda, 2004) and bacteria (Lee et al 2003). The central variable domain of the FliC protein is dispensable and can be used for the insertion and display of numerous peptides and proteins (Kuwajima, 1998; Crampton et al 2007). This has been exploited by fusing the FliC protein to a number of different peptides and shown to be functional (Crampton et al 2007). Two advantages of developing the Gram-positive flagelin display system are that Gram-positive bacteria are more robust than their Gram-negative counterparts and the chimeric flagella are easily isolated from the cell surface. In this study the researchers aimed at determining limitations of the display system and evaluate amino acid content on yields and display of selected peptides. |
en |
dc.language.iso |
en |
en |
dc.publisher |
CSIR |
en |
dc.subject |
Peptides |
en |
dc.subject |
Bacterial cells |
en |
dc.subject |
Display syatem |
en |
dc.title |
To 'display' or not to 'display'- that is the peptide |
en |
dc.type |
Conference Presentation |
en |
dc.identifier.apacitation |
Crampton, M. C., Berger, E., & Louw, M. (2008). To 'display' or not to 'display'- that is the peptide. CSIR. http://hdl.handle.net/10204/2741 |
en_ZA |
dc.identifier.chicagocitation |
Crampton, Michael C, E Berger, and ME Louw. "To 'display' or not to 'display'- that is the peptide." (2008): http://hdl.handle.net/10204/2741 |
en_ZA |
dc.identifier.vancouvercitation |
Crampton MC, Berger E, Louw M, To 'display' or not to 'display'- that is the peptide; CSIR; 2008. http://hdl.handle.net/10204/2741 . |
en_ZA |
dc.identifier.ris |
TY - Conference Presentation
AU - Crampton, Michael C
AU - Berger, E
AU - Louw, ME
AB - Microbial cell surface display is the anchoring of a heterologous protein or peptide (passenger) to the outside of the cell wall as a fusion to a cell surface associated protein (carrier). This technology has been used extensively for both eukaryotic and prokaryotic systems but has mainly focused around phages (Etz et al, 2001), yeast (Kondo and Ueda, 2004) and bacteria (Lee et al 2003). The central variable domain of the FliC protein is dispensable and can be used for the insertion and display of numerous peptides and proteins (Kuwajima, 1998; Crampton et al 2007). This has been exploited by fusing the FliC protein to a number of different peptides and shown to be functional (Crampton et al 2007). Two advantages of developing the Gram-positive flagelin display system are that Gram-positive bacteria are more robust than their Gram-negative counterparts and the chimeric flagella are easily isolated from the cell surface. In this study the researchers aimed at determining limitations of the display system and evaluate amino acid content on yields and display of selected peptides.
DA - 2008-11
DB - ResearchSpace
DP - CSIR
KW - Peptides
KW - Bacterial cells
KW - Display syatem
LK - https://researchspace.csir.co.za
PY - 2008
T1 - To 'display' or not to 'display'- that is the peptide
TI - To 'display' or not to 'display'- that is the peptide
UR - http://hdl.handle.net/10204/2741
ER -
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en_ZA |