Description

Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein,

Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our high-resolution NMR results for a transmembrane protein, outer envelope protein of molar mass 16 kDa (OEP16), an amino acid transporter from the outer membrane of chloroplasts. Three-dimensional, high-resolution NMR experiments on the [superscript 13]C, [superscript 15]N, [superscript 2]H-triply-labeled protein were used to assign protein backbone resonances and to obtain secondary structure information.

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Date Created
  • 2013-10-29
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  • Text
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    Identifier
    • Digital object identifier: 10.1371/journal.pone.0078116
    • Identifier Type
      International standard serial number
      Identifier Value
      1045-3830
    • Identifier Type
      International standard serial number
      Identifier Value
      1939-1560

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    Zook, J. D., Molugu, T. R., Jacobsen, N. E., Lin, G., Soll, J., Cherry, B. R., . . . Fromme, P. (2013). High-Resolution NMR Reveals Secondary Structure and Folding of Amino Acid Transporter from Outer Chloroplast Membrane. PLoS ONE, 8(10). doi:10.1371/journal.pone.0078116

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