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Design of a Conformation-Sensitive Xenon-Binding Cavity in the Ribose-Binding Protein

Authors

  • Thomas J. Lowery,

    1. Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA
    2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA, Fax: (+1) 510-486-6059
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  • Seth M. Rubin Dr.,

    1. Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA
    2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA, Fax: (+1) 510-486-6059
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  • E. Janette Ruiz Dr.,

    1. Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA
    2. Material Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA
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  • Alexander Pines Prof.,

    1. Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA
    2. Material Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA
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  • David E. Wemmer Prof.

    1. Department of Chemistry, University of California at Berkeley, Berkeley, CA 94720, USA
    2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, Berkeley, CA 94720, USA, Fax: (+1) 510-486-6059
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  • This work was supported by the Director, U.S. Department of Energy, under Contract No. DE-AC03-76F00098, through the Office of Naval Research (MDI-II), and through the Laboratory Directorate Research and Development Program of Lawrence Berkeley National Laboratory. We thank Prof. S. Mowbray for the ribose-binding-protein gene, H. Yokota for helpful advice with cloning, Dr. S. Burley for the pSKB3 plasmid, Dr. D. King for mass spectrometry, Prof. S. Marqusee and Dr. C. Park for providing an isothermal titration calorimeter and guidance with urea melt experiments. S.M.R. acknowledges the National Science Foundation and E.J.R. Lucent Technologies/Bell Laboratories for predoctoral fellowships.

Abstract

original image

129Xe-NMR-Spektroskopie trifft Protein-Engineering: NMR-Spektroskopie mit Laser-polarisiertem 129Xe hilft nur beim Nachweis von Proteinkonformationen, wenn das Protein über eine konformativ empfindliche Xenon bindende Kavität verfügt. Diese fehlt jedoch vielen Proteinen. Der vorgestellte Designprozess führte zu einer entsprechenden Kavität im Ribose bindenden Protein (siehe Bild) und damit zum 129Xe-NMR-spektroskopischen Nachweis von Proteinkonformation und Ligandenbindung.

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