固相合成 C 末端肽文库以研究酶蛋白异戊二烯化的特异性。
Solid-phase synthesis of C-terminal peptide libraries for studying the specificity of enzymatic protein prenylation.
机构信息
Department of Chemistry, University of Minnesota, 207 Pleasant Street, S. E. Minneapolis, MN 55455, USA.
出版信息
Chem Commun (Camb). 2012 Aug 25;48(66):8228-30. doi: 10.1039/c2cc31713c. Epub 2012 Jul 11.
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.
摘要
prenylation 是所有真核生物中一种必需的翻译后修饰。在这里，我们描述了一种在纤维素膜上含有游离 C 末端的 340 个肽的文库的合成。然后，使用该文库来探测酿酒酵母蛋白法尼基转移酶的特异性。
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