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Eric M. Brustad
Researcher at University of North Carolina at Chapel Hill
Publications - 46
Citations - 3131
Eric M. Brustad is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Amino acid & Heme. The author has an hindex of 25, co-authored 45 publications receiving 2749 citations. Previous affiliations of Eric M. Brustad include Scripps Research Institute & Illumina.
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Journal ArticleDOI
Olefin Cyclopropanation via Carbene Transfer Catalyzed by Engineered Cytochrome P450 Enzymes
TL;DR: E engineered variants of cytochrome P450BM3 that catalyze highly diastereo- and enantioselective cyclopropanation of styrenes from diazoester reagents via putative carbene transfer are reported, highlighting the capacity to adapt existing enzymes for the catalysis of synthetically important reactions not previously observed in nature.
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A Serine-Substituted P450 Catalyzes Highly Efficient Carbene Transfer to Olefins In Vivo
Pedro S. Coelho,Z. Jane Wang,Maraia E. Ener,Stefanie A. Baril,Arvind Kannan,Frances H. Arnold,Eric M. Brustad +6 more
TL;DR: A unique serine-heme ligated cytochrome “P411” that catalyzes efficient and selective carbene transfers from diazoesters to olefins in intact Escherichia coli cells is designed.
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Optimizing non-natural protein function with directed evolution
TL;DR: A marriage of ingenuity and evolution will expand the scope of protein function well beyond Mother Nature's designs.
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Site-directed spin labeling of a genetically encoded unnatural amino acid
Mark R. Fleissner,Eric M. Brustad,Eric M. Brustad,Tamás Kálai,Christian Altenbach,Duilio Cascio,Francis B. Peters,Kálmán Hideg,Sebastian Peuker,Peter G. Schultz,Wayne L. Hubbell +10 more
TL;DR: In this article, an orthogonal labeling strategy was proposed to make SDSL amenable to any protein, i.e., one that does not rely on any of the functional groups found in the common 20 amino acids.
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A General and Efficient Method for the Site-Specific Dual-Labeling of Proteins for Single Molecule Fluorescence Resonance Energy Transfer
TL;DR: A genetically encoded unnatural ketone amino acid was labeled with a hydroxylamine-containing fluorophore with high yield and specificity, allowing the study of T4 lysozyme folding at single-molecule resolution.