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Structural Origin of the High Affinity of a Chemically Evolved Lanthanide‐Binding Peptide
199
Citations
19
References
2004
Year
Crystal StructurePeptide EngineeringMolecular BiologyPeptide ScienceChemical BiologyTb3+ IonStructural OriginProtein FoldingProtein X-ray CrystallographyStructure ElucidationLuminescence-lifetime MeasurementsProtein ChemistryBiochemistryMolecular ModelingCrystallographyStructural BiologyNatural SciencesPeptide LibraryPeptide SynthesisMedicineHigh Affinity
Playing tag with terbium: New hydrophobic contacts and ligating amino acids are revealed in the 2.0-Å resolution X-ray crystal structure of a chemically evolved 17-residue lanthanide-binding peptide complexed with a Tb3+ ion (see ribbon diagram). The crystal structure agrees well with luminescence-lifetime measurements in solution, which indicate that no first-shell-coordinating water molecules are present in the complex. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2004/z460028_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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