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Science. 2002 May 31;296(5573):1700-3.

Probing protein electrostatics with a synthetic fluorescent amino acid.

Author information

1
Howard Hughes Medical Institute and Departments of Physiology and Biochemistry, University of California San Francisco, San Francisco, CA 94143, USA. bcohen@itsa.ucsf.edu

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.

PMID:
12040199
DOI:
10.1126/science.1069346
[Indexed for MEDLINE]
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