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Validation of the Binding Site Structure of the Cellular Retinol-Binding Protein (CRBP) by Ligand NMR Chemical Shift Perturbations
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    Validation of the Binding Site Structure of the Cellular Retinol-Binding Protein (CRBP) by Ligand NMR Chemical Shift Perturbations
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    Department of Chemistry, The Pennsylvania State University, 104 Chemistry Building, University Park, Pennsylvania 16802
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2005, 127, 15, 5310–5311
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    https://doi.org/10.1021/ja042616k
    Published March 26, 2005
    Copyright © 2005 American Chemical Society

    Abstract

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    We have calculated proton chemical shift perturbations (CSPs) of retinol in the cellular retinol-binding protein (CRBP) through the use of a recently developed computational approach (Wang et al. J. Chem. Phys.2004, 120, 11392−11400). Excellent agreement with experimental values was obtained for the X-ray structure, whereas the lack of a key hydrogen bond and the distorted isoprene tail of retinol for some NMR models lead to large CSP RMSDs. Therefore, a comparison of computed CSPs of retinol with experiment offers a convenient way to validate the structure of retinol and its orientation in the binding site for the NMR structures.

    Copyright © 2005 American Chemical Society

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    Cited By

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    This article is cited by 12 publications.

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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2005, 127, 15, 5310–5311
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja042616k
    Published March 26, 2005
    Copyright © 2005 American Chemical Society

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