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Protein structure / Spectroscopy / Biochemistry / Protein methods / Nuclear magnetic resonance spectroscopy of proteins / Turn / Peptide / Heteronuclear single-quantum correlation spectroscopy / Nuclear magnetic resonance spectroscopy / Nuclear magnetic resonance / Chemistry / Biology


Published on Web[removed]Hairpin Structure of a Biarsenical-Tetracysteine Motif Determined by NMR Spectroscopy Fatemeh Madani,† Jesper Lind,† Peter Damberg,† Stephen R. Adams,‡ Roger Y. Tsien,*,‡ and Astrid
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Document Date: 2014-07-01 03:39:59


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L. A. / Burlington / New York / /

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Wiley & Sons / Elsevier Academic Press / Dexter / BioMagResBank / Arrhenius Laboratories / /

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United States / /

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Howard Hughes Medical Institute / Phe1 complex / ReAsH complex / UniVersity of California / Stockholm UniVersity / /

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chemical shifts8 / chemical shift list / 13C chemical shifts / biological applications / secondary chemical shifts / low-energy structures / 1H chemical shifts / aqueous solution / /

Organization

Swedish Research Council / Stockholm UniVersity / National Institute of Health / Knut and Alice Wallenberg Foundation / G7 / NMR Spectroscopy Fatemeh Madani / † Jesper Lind / † Peter Damberg / † Stephen R. Adams / ‡ Roger Y. Tsien / * / ‡ and Astrid O. Gra¨slund* / † Department of Biochemistry / Howard Hughes Medical Institute / UniVersity of California / San Diego / /

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Stephen R. Adams / ‡ Roger / Roger Y. Tsien / Peter Damberg / † Stephen / Fatemeh Madani / Astrid O. Gra / /

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California / Massachusetts / /

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JA809315X J. AM / J. AM / 4614 J. AM / /

Technology

crystallization / Spectroscopy / FlAsH / /

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http /

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