Please use this identifier to cite or link to this item: https://doi.org/10.1002/chem.200400414
Title: Expanded utility of the native chemical ligation reaction
Authors: Yeo, D.S.Y.
Srinivasan, R.
Chen, G.Y.J. 
Yao, S.Q. 
Keywords: Bioimaging
Biotinylation
Fluorescence
Intein
Native chemical ligation
Protein modifications
Issue Date: 4-Oct-2004
Source: Yeo, D.S.Y., Srinivasan, R., Chen, G.Y.J., Yao, S.Q. (2004-10-04). Expanded utility of the native chemical ligation reaction. Chemistry - A European Journal 10 (19) : 4664-4672. ScholarBank@NUS Repository. https://doi.org/10.1002/chem.200400414
Abstract: The post-genomic era heralds a multitude of challenges for chemists and biologists alike, with the study of protein functions at the heart of much research. The elucidation of protein structure, localization, stability, post-translational modifications, and protein interactions will steadily unveil the role of each protein and its associated biological function in the cell. The push to develop new technologies has necessitated the integration of various disciplines in science. Consequently, the role of chemistry has never been so profound in the study of biological processes. By combining the strengths of recombinant DNA technology, protein splicing, organic chemistry, and the chemoselective chemistry of native chemical ligation, various strategies have been successfully developed and applied to chemo-selectively label proteins, both in vitro and in live cells, with biotin, fluorescent, and other small molecule probes. The site-specific incorporation of molecular entities with unique chemical functionalities in proteins has many potential applications in chemical and biological studies of proteins. In this article, we highlight recent progress of these strategies in several areas related to proteomics and chemical biology, namely, in vitro and in vivo protein biotinylation, protein microarray technologies for large-scale protein analysis, and live-cell bioimaging.
Source Title: Chemistry - A European Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/77604
ISSN: 09476539
DOI: 10.1002/chem.200400414
Appears in Collections:Staff Publications

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