Native chemical ubiquitination using a genetically incorporated azidonorleucine

Native chemical ubiquitination using a genetically incorporated azidonorleucine

A robust chemical ubiquitination method was developed. The method employed a genetically incorporated azidonorleucine as an orthogonal lysine precursor for the installation of a Gly residue bearing an Nα-auxiliary which mediated the ligation between ubiquitin(1–75)-thioester and the target protein....

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Main Authors: Yang, Renliang, Bi, Xiaobao, Li, Fupeng, Cao, Yuan, Liu, Chuan-Fa
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2016
Subjects:
Biological Sciences
Online Access:https://hdl.handle.net/10356/82021
http://hdl.handle.net/10220/39753
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Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-82021
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spelling sg-ntu-dr.10356-820212023-02-28T16:58:05Z Native chemical ubiquitination using a genetically incorporated azidonorleucine Yang, Renliang Bi, Xiaobao Li, Fupeng Cao, Yuan Liu, Chuan-Fa School of Biological Sciences Biological Sciences A robust chemical ubiquitination method was developed. The method employed a genetically incorporated azidonorleucine as an orthogonal lysine precursor for the installation of a Gly residue bearing an Nα-auxiliary which mediated the ligation between ubiquitin(1–75)-thioester and the target protein. To demonstrate our methodology, a model protein, K48-linked diubiquitin, was synthesized with an overall yield of 35%. ASTAR (Agency for Sci., Tech. and Research, S’pore) Accepted version 2016-01-22T03:58:42Z 2019-12-06T14:44:51Z 2016-01-22T03:58:42Z 2019-12-06T14:44:51Z 2014 Journal Article Yang, R., Bi, X., Li, F., Cao, Y., & Liu, C.-F. (2014). Native chemical ubiquitination using a genetically incorporated azidonorleucine. Chemical Communications, 50(59), 7971-7974. 1359-7345 https://hdl.handle.net/10356/82021 http://hdl.handle.net/10220/39753 10.1039/c4cc03721a en Chemical Communications © 2014 The Royal Society of Chemistry. This is the author created version of a work that has been peer reviewed and accepted for publication by Chemical Communications, The Royal Society of Chemistry. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1039/c4cc03721a]. 4 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Biological Sciences
spellingShingle Biological Sciences
Yang, Renliang
Bi, Xiaobao
Li, Fupeng
Cao, Yuan
Liu, Chuan-Fa
Native chemical ubiquitination using a genetically incorporated azidonorleucine
description A robust chemical ubiquitination method was developed. The method employed a genetically incorporated azidonorleucine as an orthogonal lysine precursor for the installation of a Gly residue bearing an Nα-auxiliary which mediated the ligation between ubiquitin(1–75)-thioester and the target protein. To demonstrate our methodology, a model protein, K48-linked diubiquitin, was synthesized with an overall yield of 35%.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Yang, Renliang
Bi, Xiaobao
Li, Fupeng
Cao, Yuan
Liu, Chuan-Fa
format Article
author Yang, Renliang
Bi, Xiaobao
Li, Fupeng
Cao, Yuan
Liu, Chuan-Fa
author_sort Yang, Renliang
title Native chemical ubiquitination using a genetically incorporated azidonorleucine
title_short Native chemical ubiquitination using a genetically incorporated azidonorleucine
title_full Native chemical ubiquitination using a genetically incorporated azidonorleucine
title_fullStr Native chemical ubiquitination using a genetically incorporated azidonorleucine
title_full_unstemmed Native chemical ubiquitination using a genetically incorporated azidonorleucine
title_sort native chemical ubiquitination using a genetically incorporated azidonorleucine
publishDate 2016
url https://hdl.handle.net/10356/82021
http://hdl.handle.net/10220/39753
_version_ 1759856891848032256

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