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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Slaving: Solvent fluctuations dominate protein dynamics and functions
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Self-citation
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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