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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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Cited by
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Fenimore, P. W., Frauenfelder, H., McMahon, B. H., & Parak, F. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.212637899 · Cited by 677
Smart polymeric gels: Redefining the limits of biomedical devices
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
Monitoring 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
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
- 0
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- closed
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