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Abstract
The de novo design of artificial metalloproteins from first-principles is a powerful strategy with which to establish the minimum structure required for function, as well as to identify the important design features for tuning the chemistry of the coordinated metal ion. Herein we describe recent contributions to this field, covering metallo-porphyrin, mononuclear and multinuclear metal ion sites engineered into de novo proteins. Using miniature artificial scaffolds these examples demonstrate that complex natural protein folds are not required to mimic naturally occurring metal ion sites in proteins. More importantly progress is being made to engineer de novo metalloproteins capable of performing functions not in the repertoire of biology.
Original language | English |
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Pages (from-to) | 934-939 |
Journal | Current Opinion in Chemical Biology |
Volume | 17 |
Issue number | 6 |
Early online date | 31 Oct 2013 |
DOIs | |
Publication status | Published - 1 Dec 2013 |
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Dive into the research topics of 'Incorporating metals into de novo proteins'. Together they form a unique fingerprint.Projects
- 1 Finished
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Ferrocene-Peptide Adducts for DNA Binding: Towards Sequence-Selective Electrochemical DNA Sensors
Peacock, A. (Principal Investigator)
Engineering & Physical Science Research Council
16/04/12 → 15/04/13
Project: Research Councils