The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Probing Protein Electrostatics with a Synthetic Fluorescent Amino Acid
Abstract
Electrostatics affect virtually all aspects of protein structure and activity and are particularly important in proteins whose primary function is to stabilize charge. Here we introduce a fluorescent amino acid, Aladan, which can probe the electrostatic character of a protein at multiple sites. Aladan is exceptionally sensitive to the polarity of its surroundings and can be incorporated site-selectively at buried and exposed sites, in both soluble and membrane proteins. Steady-state and time-resolved fluorescence measurements of Aladan residues at different buried and exposed sites in the B1 domain of protein G suggest that its interior is polar and heterogeneous.
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Cites
Principles of Fluorescence Spectroscopy
Lakowicz, J. R. (1999) · Springer eBooks · doi:10.1007/978-1-4757-3061-6 · Cited by 26,947
Subpicosecond Measurements of Polar Solvation Dynamics: Coumarin 153 Revisited
Horng, M. L., Gardecki, J. A., Papazyan, A., & Maroncelli, M. (1995) · The Journal of Physical Chemistry · doi:10.1021/j100048a004 · Cited by 2,087
Expanding the Genetic Code of Escherichia coli
Wang, L., Brock, A., Herberich, B., & Schultz, P. G. (2001) · Science · doi:10.1126/science.1060077 · Cited by 1,499
Expressed protein ligation: A general method for protein engineering
Muir, T. W., Sondhi, D., & Cole, P. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.12.6705 · Cited by 1,189
Calculations of electrostatic interactions in biological systems and in solutions
Warshel, A., & Russell, S. T. (1984) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583500005333 · Cited by 995
What are the dielectric “constants” of proteins and how to validate electrostatic models?
Schutz, C. N., & Warshel, A. (2001) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.1106 · Cited by 942
Weber, G., & Farris, F. J. (1979) · Biochemistry · doi:10.1021/bi00581a025 · Cited by 854
A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G
Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816
Pal, S. K., Peon, J., & Zewail, A. H. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042697899 · Cited by 549
Design, structure and stability of a hyperthermophilic protein variant
Malakauskas, S. M., & Mayo, S. L. (1998) · Nature Structural Biology · doi:10.1038/nsb0698-470 · Cited by 350
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Chaterji, S., Kwon, I. K., & Park, K. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.05.018 · Cited by 615
Szeto, H. H. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12461 · Cited by 548
Birk, A. V., Liu, S., Soong, Y., Mills, W., Singh, P., Warren, J. D., Seshan, S. V., Pardee, J. D., & Szeto, H. H. (2013) · Journal of the American Society of Nephrology · doi:10.1681/asn.2012121216 · Cited by 479
Electric Fields and Enzyme Catalysis
Fried, S. D., & Boxer, S. G. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044432 · Cited by 465
Self-citationMonitoring protein interactions and dynamics with solvatochromic fluorophores
Loving, G. S., Sainlos, M., & Imperiali, B. (2010) · Trends in Biotechnology · doi:10.1016/j.tibtech.2009.11.002 · Cited by 305
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Curutchet, C., Muñoz-Losa, A., Monti, S., Kongsted, J., Scholes, G. D., & Mennucci, B. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct9001366 · Cited by 298
A genetically encoded fluorescent amino acid
Summerer, D., Chen, S., Wu, N., Deiters, A., Chin, J. W., & Schultz, P. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603965103 · Cited by 273
A structural remedy toward bright dipolar fluorophores in aqueous media
Singha, S., Kim, D., Roy, B., Sambasivan, S., Moon, H., Rao, A. S., Kim, J. Y., Joo, T., Park, J. W., Rhee, Y. M., et al. (2015) · Chemical Science · doi:10.1039/c5sc01076d · Cited by 170
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
Dynamics and mechanisms of DNA repair by photolyase
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Metadata
- Authors
- Cohen, B. E., McAnaney, T. B., Park, E. S., Jan, Y. N., Boxer, S. G., & Jan, L. Y.
- Venue
- Science
- Published
- 2002-05-31
- Volume
- 296
- Issue
- 5573
- Pages
- 1700-1703
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2015745958
- Cited by
- 381
- References
- 23
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.