Heterochromia in designed metallopeptides: Geometry-selective binding of CdII in a de novo peptide

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Abstract

Molecular recognition and control of the physical properties of metal ions are major challenges in metalloprotein design. The newly designed peptide Grand L16PenL26AL30C binds two CdII ions, each with a different coordination geometry - trigonal planar or pseudotetrahedral (see picture; Cd purple, S yellow, O blue). The physical properties of the two centers, such as site selectivity and pH dependence of binding, differ as well. (Graph Presented) © 2007 Wiley-VCH Verlag GmbH &. Co. KGaA.

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Iranzo, O., Cabello, C., & Pecoraro, V. L. (2007). Heterochromia in designed metallopeptides: Geometry-selective binding of CdII in a de novo peptide. Angewandte Chemie - International Edition, 46(35), 6688–6691. https://doi.org/10.1002/anie.200701729

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