Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation

Yen Chih Wang; Mark D. Distefano

doi:10.1039/c2cc31713c

Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation

Yen Chih Wang, Mark D. Distefano

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	8228-8230
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	66
DOIs	https://doi.org/10.1039/c2cc31713c
State	Published - Jul 23 2012

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title = "Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation",

abstract = "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.",

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Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation

Abstract

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