The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
FTIR analysis of GPCR activation using azido probes
Open accessAbstract
We demonstrate the site-directed incorporation of an IR-active amino acid, p-azido-l-phenylalanine (azidoF, 1), into the G protein–coupled receptor rhodopsin using amber codon suppression technology. The antisymmetric stretch vibration of the azido group absorbs at ~2,100 cm−1 in a clear spectral window and is sensitive to its electrostatic environment. We used FTIR difference spectroscopy to monitor the azido probe and show that the electrostatic environments of specific interhelical networks change during receptor activation.
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Cites
Crystal structure of opsin in its G-protein-interacting conformation
Scheerer, P., Park, J. H., Hildebrand, P. W., Kim, Y. J., Krauß, N., Choe, H.-W., Hofmann, K. P., & Ernst, O. P. (2008) · Nature · doi:10.1038/nature07330 · Cited by 1,059
A General Method for Site-specific Incorporation of Unnatural Amino Acids into Proteins
Noren, C. J., Anthony-Cahill, S. J., Griffith, M. C., & Schultz, P. G. (1989) · Science · doi:10.1126/science.2649980 · Cited by 1,019
Cited by
Adding New Chemistries to the Genetic Code
Liu, C. C., & Schultz, P. G. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.105824 · Cited by 1,725
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz-Fonfria, V. A. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 325
Labeling and Single-Molecule Methods To Monitor G Protein-Coupled Receptor Dynamics
Tian, H., Fürstenberg, A., & Huber, T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00084 · Cited by 114
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Metadata
- Authors
- Ye, S., Huber, T., Vogel, R., & Sakmar, T. P.
- Venue
- Nature Chemical Biology
- Published
- 2009-04-26
- Volume
- 5
- Issue
- 6
- Pages
- 397-399
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W1977360823
- Cited by
- 182
- References
- 2
- FWCI
- 6.36
- Type
- journal article
- Language
- en
- Open access
- green
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