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To 'display' or not to 'display'- that is the peptide

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dc.contributor.author Crampton, Michael C
dc.contributor.author Berger, E
dc.contributor.author Louw, ME
dc.date.accessioned 2008-12-12T12:24:13Z
dc.date.available 2008-12-12T12:24:13Z
dc.date.issued 2008-11
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
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 - en_ZA


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