| Literature DB >> 32144673 |
Caroline E Weller1, Champak Chatterjee2.
Abstract
The posttranslational modification of cellular proteins by ubiquitin (Ub), called ubiquitylation, is indispensable for the normal growth and development of eukaryotic organisms. In order to conduct studies that elucidate the precise mechanistic roles for Ub, access to site-specifically and homogenously ubiquitylated proteins and peptides is critical. However, the low abundance, heterogeneity, and dynamic nature of protein ubiquitylation are significant limitations toward such studies. Here we provide a facile expressed protein ligation method that does not require specialized apparatus and permits the rapid semisynthesis of ubiquitylated peptides by using the atom-efficient ligation auxiliary 2-aminooxyethanethiol.Entities:
Keywords: Auxiliary; Ligation; Peptide; Semisynthesis; Sumoylation; Ubiquitin; Ubiquitylation
Year: 2020 PMID: 32144673 PMCID: PMC7604904 DOI: 10.1007/978-1-0716-0434-2_14
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745