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. cerevisiae.
Department of Chemistry, University of Minnesota, 207 Pleasant Street, S. E. Minneapolis, MN 55455, USA.
Yen-Chih
YC
Wang
Mark D
MD
Distefano
D051231:Farnesyltranstransferase / Q000737:chemistry; D015394:Molecular Structure; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis*; D017368:Protein Prenylation; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D060327:Solid-Phase Synthesis Techniques; D013379:Substrate Specificity
D019151:Peptide Library; D010455:Peptides; D051231:Farnesyltranstransferase