Published January 26, 2005
| Supplemental Material
Journal Article
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Caged Phosphoproteins
Abstract
We present the chemical and biological synthesis of caged phosphoproteins using the in vitro nonsense codon suppression methodology. Specifically, phosphoamino acid analogues of serine, threonine, and tyrosine with a single photocleavable o-nitrophenylethyl caging group were synthesized as the amino acyl tRNA adducts for insertion into full-length proteins. For this purpose, a novel phosphitylating agent was developed. The successful incorporation of these bulky and charged amino acids into the α-subunit of the nicotinic acetyl choline receptor (nAChR) and the vasodilator-stimulated phosphoprotein (VASP) using an in vitro translation system is reported.
Additional Information
© 2005 American Chemical Society. Received 7 October 2004. Published online 30 December 2004. Published in print 1 January 2005. The work has been supported by the Cell Migration Consortium Grant GM64346 to B.I., NS-34407 to D.A.D, and the HFSP Foundation for M.E.V. The authors thank Professor F. Gertler for the VASP gene and antibody.Attached Files
Supplemental Material - ja043875csi20041119_112107.pdf
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Additional details
- Eprint ID
- 76742
- DOI
- 10.1021/ja043875c
- Resolver ID
- CaltechAUTHORS:20170420-063814654
- GM64346
- NIH
- NS-34407
- NIH
- Human Frontier Science Program
- Created
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2017-04-20Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field