BIOL 197 |
| Lanthanide-Binding Tags (LBTs) are peptide sequences of twenty amino acids or fewer that were chemically evolved from native calcium-binding loops to bind lanthanide ions tightly and selectively. LBTs can be easily incorporated into any protein using standard molecular biology techniques, and feature an optimally placed tryptophan residue as a sensitizer of terbium luminescence. Addition of lanthanide ion thereby enables site-specific integration of these powerful biophysical probes for use in conjunction with techniques including luminescence- and NMR-spectroscopy and X-ray crystallography. Concatenation of two lanthanide-binding motifs now affords a “double Lanthanide-Binding Tag” (dLBT). This ability to simultaneously bind pairs of lanthanide ions yields an improved tag, including twice the anisotropic magnetic susceptibility and anomalous scattering power of single lanthanide-binding moieties, and at least twice the luminescence output of the progenitor LBT. Furthermore, biophysical studies reveal that the larger peptide structure of the dLBT is more ordered with respect to the tagged protein.
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Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Biological Chemistry |
