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| Content Provider | PubMed Central |
|---|---|
| Author | Lester, Henry A. Davidson, Norman Dougherty, Dennis A. England, Pamela M. |
| Copyright Year | 1997 |
| Abstract | A method for site-specific, nitrobenzyl-induced photochemical proteolysis of diverse proteins expressed in living cells has been developed based on the chemistry of the unnatural amino acid (2-nitrophenyl)glycine (Npg). Using the in vivo nonsense codon suppression method for incorporating unnatural amino acids into proteins expressed in Xenopus oocytes, Npg has been incorporated into two ion channels: the Drosophila Shaker B K+ channel and the nicotinic acetylcholine receptor. Functional studies in vivo show that irradiation of proteins containing an Npg residue does lead to peptide backbone cleavage at the site of the novel residue. Using this method, evidence is obtained for an essential functional role of the “signature” Cys128–Cys142 disulfide loop of the nAChR α subunit. |
| Starting Page | 11025 |
| File Format | |
| ISSN | 10916490 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 20 |
| Volume Number | 94 |
| Language | English |
| Publisher | The National Academy of Sciences of the USA |
| Publisher Date | 1997-09-30 |
| Access Restriction | Open |
| Rights Holder | The National Academy of Sciences of the USA |
| Subject Keyword | Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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