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      100% complete assignment of non-labile 1H, 13C, and 15N signals for calcium-loaded calbindin D 9k P43G

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          Abstract

          Here we present the 100% complete assignment chemical shift of non-labile 1H, 15N and 13C nuclei of Calbindin D 9k P43G. The assignment includes all non-exchangeable side chain nuclei, including ones that are rarely reported, such as LysNζ as well as the termini. NMR experiments required to achieve truly complete assignments are discussed. To the best of our knowledge our assignments for Calbindin D 9k extend beyond previous studies reaching near-completeness (Vis et al. in Biochem 33:14858–14870, 1994; Yamazaki et al. in J Am Chem Soc 116:6464–6465, 1994; Yamazaki et al. in Biochem 32:5656–5669, 1993b).

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          Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity

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            Carp muscle calcium-binding protein. II. Structure determination and general description.

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              Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.

              The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples of the SH3 in near physiological buffer exhibiting an approximately 1:1 ratio of the two states. NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment.
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                Author and article information

                Contributors
                f.a.a.mulder@rug.nl
                Journal
                Biomol NMR Assign
                Biomolecular Nmr Assignments
                Springer Netherlands (Dordrecht )
                1874-2718
                1874-270X
                12 November 2010
                12 November 2010
                April 2011
                : 5
                : 1
                : 79-84
                Affiliations
                [1 ]Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
                [2 ]Department of Biophysical Chemistry, Lund University, PO Box 124, Lund, Sweden
                Article
                9272
                10.1007/s12104-010-9272-3
                3049223
                21069485
                55d2e86f-e1c7-4605-a519-f697c6d9d763
                © The Author(s) 2010
                History
                : 20 August 2010
                : 24 September 2010
                Categories
                Article
                Custom metadata
                © Springer Science+Business Media B.V. 2011

                Biophysics
                100% complete assignment,calbindin d9k,nmr spectroscopy,assignment strategy
                Biophysics
                100% complete assignment, calbindin d9k, nmr spectroscopy, assignment strategy

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