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Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals

1
Department of Chemistry, Princeton University, Princeton, NJ 08540, USA
2
Department of Molecular Biology, Princeton University, Princeton, NJ 08540, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Received: 24 September 2018 / Revised: 31 December 2018 / Accepted: 4 January 2019 / Published: 9 January 2019
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Abstract

Life as we know it would not exist without the ability of protein sequences to bind metal ions. Transition metals, in particular, play essential roles in a wide range of structural and catalytic functions. The ubiquitous occurrence of metalloproteins in all organisms leads one to ask whether metal binding is an evolved trait that occurred only rarely in ancestral sequences, or alternatively, whether it is an innate property of amino acid sequences, occurring frequently in unevolved sequence space. To address this question, we studied 52 proteins from a combinatorial library of novel sequences designed to fold into 4-helix bundles. Although these sequences were neither designed nor evolved to bind metals, the majority of them have innate tendencies to bind the transition metals copper, cobalt, and zinc with high nanomolar to low-micromolar affinity. View Full-Text
Keywords: protein design; novel metalloproteins; binary patterned amino acid sequences; prebiotic chemistry protein design; novel metalloproteins; binary patterned amino acid sequences; prebiotic chemistry
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Wang, M.S.; Hoegler, K.J.; Hecht, M.H. Unevolved De Novo Proteins Have Innate Tendencies to Bind Transition Metals. Life 2019, 9, 8.

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