ArticleAccounts of chemical research2019
Noncoded Amino Acids in de Novo Metalloprotein Design: Controlling Coordination Number and Catalysis.
Article in Accounts of chemical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Metallo-coiled Coil Stabilization via Chemical Cross-Linking: Implications for Gd(III)-Based MRI Contrast Agents.Journal of the American Chemical Society · 2025Article
- Application of artificial backbone connectivity in the development of metalloenzyme mimics.Current opinion in chemical biology · 2024Review
- Artificial Metalloenzyme-Catalyzed Enantioselective Amidation via Nitrene Insertion in Unactivated C(Journal of the American Chemical Society · 2023Article
- Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme.RSC advances · 2022Article
- Identifying metal binding amino acids based on backbone geometries as a tool for metalloprotein engineering.Protein science : a publication of the Protein Society · 2021Article
- Artificial Metalloenzymes: From Selective Chemical Transformations to Biochemical Applications.Molecules (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The relationship between structure and function has long been one of the major points of investigation in Biophysics. Understanding how much, or how little, of a protein's often complicated structure is necessary for its function can lead to directed therapeutic strategies and would allow one to design proteins for specific desired functions. Studying protein function by de novo design builds the functionality from the ground up in a completely unrelated and noncoded protein scaffold. Our lab has used this strategy to study heavy and transition metal binding within the TRI family of three stranded coiled coil (3SCC) constructs to understand coordination geometry and metalloenzyme catalytic control within a protein environment. These peptides contain hydrophobic layers within the interior of the 3SCC, which one can mutate to metal binding residues to create a minimal metal binding site, while solid phase synthesis allows our lab to easily incorporate a number of noncoded amino acids including d enantiomers of binding or secondary coordination sphere amino acids, penicillamine, or methylated versions of histidine. Our studies of Cd(II) binding to Cys
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