Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation
Prenylation is an essential post-translational modification in all eukaryotes. Here we describe the synthesis of a 340-member library of peptides containing free C-termini on cellulose membranes. The resulting library was then used to probe the specificity of protein farnesyltransferase from S. cere...
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| Veröffentlicht in: | Chemical communications (Cambridge, England) England), 2012-01, Vol.48 (66), p.8228-8230 |
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| container_title | Chemical communications (Cambridge, England) |
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| creator | Wang, Yen-Chih Distefano, Mark D |
| description | Prenylation is an essential post-translational modification in all eukaryotes. Here we describe the synthesis of a 340-member library of peptides containing free C-termini on cellulose membranes. The resulting library was then used to probe the specificity of protein farnesyltransferase from S. cerevisiae. |
| doi_str_mv | 10.1039/c2cc31713c |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 1359-7345 |
| ispartof | Chemical communications (Cambridge, England), 2012-01, Vol.48 (66), p.8228-8230 |
| issn | 1359-7345 1364-548X 1364-548X |
| language | eng |
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| source | MEDLINE; Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection |
| subjects | cellulose chemical communication chemical compounds chemical reactions eukaryotic cells Farnesyltranstransferase - chemistry geranylgeranyl diphosphate synthase Molecular Structure peptide libraries Peptide Library Peptides - chemical synthesis post-translational modification Protein Prenylation Saccharomyces cerevisiae - enzymology Solid-Phase Synthesis Techniques Substrate Specificity |
| title | Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation |
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