Genetically Encoding an Electrophilic Amino Acid for Protein Stapling and Covalent Binding to Native Receptors

Covalent bonds can be generated within and between proteins by an unnatural amino acid (Uaa) reacting with a natural residue through proximity-enabled bioreactivity. Until now, Uaas have been developed to react mainly with cysteine in proteins. Here we genetically encoded an electrophilic Uaa capabl...

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Vydáno v:	ACS chemical biology Ročník 9; číslo 9; s. 1956 - 1961
Hlavní autoři:	Chen, Xiao-Hua, Xiang, Zheng, Hu, Ying S, Lacey, Vanessa K, Cang, Hu, Wang, Lei
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States American Chemical Society 19.09.2014
Témata:	Amino Acyl-tRNA Synthetases - genetics Amino Acyl-tRNA Synthetases - metabolism Cross-Linking Reagents - chemistry Cysteine - chemistry Histidine - chemistry Histidine - genetics Humans Lysine - chemistry Lysine - genetics Methanosarcina - genetics Methanosarcina - metabolism Myoglobin - genetics Myoglobin - metabolism Protein Binding Protein Conformation Protein Engineering - methods Receptor, ErbB-2 - chemistry Receptor, ErbB-2 - metabolism Recombinant Proteins - chemistry Recombinant Proteins - metabolism
ISSN:	1554-8929, 1554-8937, 1554-8937
On-line přístup:	Získat plný text
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