@article{Widder2019-05-17Doubl-45999,
  year={2019},
  doi={10.1021/acschembio.8b01111},
  title={Double Nitroxide Labeling by Copper-Catalyzed Azide–Alkyne Cycloadditions with Noncanonical Amino Acids for Electron Paramagnetic Resonance Spectroscopy},
  number={5},
  volume={14},
  issn={1554-8929},
  journal={ACS Chemical Biology},
  pages={839--844},
  author={Widder, Pia and Berner, Frederic and Summerer, Daniel and Drescher, Malte}
}

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    <dc:contributor>Widder, Pia</dc:contributor>
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    <dc:creator>Berner, Frederic</dc:creator>
    <dc:contributor>Summerer, Daniel</dc:contributor>
    <dc:creator>Drescher, Malte</dc:creator>
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    <dc:contributor>Berner, Frederic</dc:contributor>
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    <dcterms:abstract xml:lang="eng">Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling (SDSL) is an important tool to obtain long-range distance restraints for protein structural research. We here study a variety of azide- and alkyne-bearing noncanonical amino acids (ncAA) in terms of protein single- and double-incorporation efficiency via nonsense suppression, metabolic stability, yields of nitroxide labeling via copper-catalyzed [3 + 2] azide–alkyne cycloadditions (CuAAC), and spectroscopic properties in continuous-wave and double electron–electron resonance measurements. We identify para-ethynyl-l-phenylalanine and para-propargyloxy-l-phenylalanine as suitable ncAA for CuAAC-based SDSL that will complement current SDSL approaches, particularly in cases in which essential cysteines of a target protein prevent the use of sulfhydryl-reactive spin labels.</dcterms:abstract>
    <dc:creator>Summerer, Daniel</dc:creator>
    <dc:contributor>Drescher, Malte</dc:contributor>
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    <dcterms:title>Double Nitroxide Labeling by Copper-Catalyzed Azide–Alkyne Cycloadditions with Noncanonical Amino Acids for Electron Paramagnetic Resonance Spectroscopy</dcterms:title>
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