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    De Novo Design of a Single-Chain Diphenylporphyrin Metalloprotein

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    nihms62637.pdf (2.358Mb)
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    https://pubs.acs.org/doi/10.1021/ja071199j
    Permanent Link
    https://doi.org/10.1021/ja071199j
    http://hdl.handle.net/11603/21409
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    • UMBC Computer Science and Electrical Engineering Department
    • UMBC Office for the Vice President of Research
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    Author/Creator
    Bender, Gretchen M.
    Lehmann, Andreas
    Zou, Hongling
    Cheng, Hong
    Fry, H. Christopher
    Engel, Don
    Therien, Michael J.
    Blasie, J. Kent
    Roder, Heinrich
    Saven, Jeffrey G.
    DeGrado, William F.
    Date
    2007-08-10
    Type of Work
    20 pages
    Text
    journal articles preprints
    Citation of Original Publication
    Bender et al., De Novo Design of a Single-Chain Diphenylporphyrin Metalloprotein, J Am Chem Soc. 2007 September 5; 129(35): 10732–10740. doi:10.1021/ja071199j.
    Rights
    This item is likely protected under Title 17 of the U.S. Copyright Law. Unless on a Creative Commons license, for uses protected by Copyright Law, contact the copyright holder or the author.
    This document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Journal of the American Chemical Society, copyright © American Chemical Society after peer review. To access the final edited and published work see https://doi.org/10.1021/ja071199j.
    Abstract
    We describe the computational design of a single-chain four-helix bundle that noncovalently self-assembles with fully synthetic non-natural porphyrin cofactors. With this strategy, both the electronic structure of the cofactor as well as its protein environment may be varied to explore and modulate the functional and photophysical properties of the assembly. Solution characterization (NMR, UV−vis) of the protein showed that it bound with high specificity to the desired cofactors, suggesting that a uniquely structured protein and well-defined site had indeed been created. This provides a genetically expressed single-chain protein scaffold that will allow highly facile, flexible, and asymmetric variations to enable selective incorporation of different cofactors, surface-immobilization, and introduction of spectroscopic probes.


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    Albin O. Kuhn Library & Gallery
    University of Maryland, Baltimore County
    1000 Hilltop Circle
    Baltimore, MD 21250
    www.umbc.edu/scholarworks

    Contact information:
    Email: scholarworks-group@umbc.edu
    Phone: 410-455-3021


    If you wish to submit a copyright complaint or withdrawal request, please email mdsoar-help@umd.edu.