Probing Protein Electrostatics with a Synthetic Fluorescent Amino Acid

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Science  31 May 2002:
Vol. 296, Issue 5573, pp. 1700-1703
DOI: 10.1126/science.1069346

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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.

  • * These authors contributed equally to this work.

  • To whom correspondence should be addressed. Email: bcohen{at}

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