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492 related items for PubMed ID: 11828455

  • 1. Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla.
    Pauli J, Baldus M, van Rossum B, de Groot H, Oschkinat H.
    Chembiochem; 2001 Apr 02; 2(4):272-81. PubMed ID: 11828455
    [Abstract] [Full Text] [Related]

  • 2. Measurement of multiple psi torsion angles in uniformly 13C,15N-labeled alpha-spectrin SH3 domain using 3D 15N-13C-13C-15N MAS dipolar-chemical shift correlation spectroscopy.
    Ladizhansky V, Jaroniec CP, Diehl A, Oschkinat H, Griffin RG.
    J Am Chem Soc; 2003 Jun 04; 125(22):6827-33. PubMed ID: 12769594
    [Abstract] [Full Text] [Related]

  • 3. Determination of solid-state NMR structures of proteins by means of three-dimensional 15N-13C-13C dipolar correlation spectroscopy and chemical shift analysis.
    Castellani F, van Rossum BJ, Diehl A, Rehbein K, Oschkinat H.
    Biochemistry; 2003 Oct 07; 42(39):11476-83. PubMed ID: 14516199
    [Abstract] [Full Text] [Related]

  • 4. Assignment of the nonexchanging protons of the alpha-spectrin SH3 domain by two- and three-dimensional 1H-13C solid-state magic-angle spinning NMR and comparison of solution and solid-state proton chemical shifts.
    van Rossum BJ, Castellani F, Rehbein K, Pauli J, Oschkinat H.
    Chembiochem; 2001 Dec 03; 2(12):906-14. PubMed ID: 11948879
    [Abstract] [Full Text] [Related]

  • 5. Assignment of amide proton signals by combined evaluation of HN, NN and HNCA MAS-NMR correlation spectra.
    van Rossum BJ, Castellani F, Pauli J, Rehbein K, Hollander J, de Groot HJ, Oschkinat H.
    J Biomol NMR; 2003 Mar 03; 25(3):217-23. PubMed ID: 12652133
    [Abstract] [Full Text] [Related]

  • 6. Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR.
    Hong M.
    J Biomol NMR; 1999 Sep 03; 15(1):1-14. PubMed ID: 10549131
    [Abstract] [Full Text] [Related]

  • 7. Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins.
    Higman VA, Flinders J, Hiller M, Jehle S, Markovic S, Fiedler S, van Rossum BJ, Oschkinat H.
    J Biomol NMR; 2009 Aug 03; 44(4):245-60. PubMed ID: 19609683
    [Abstract] [Full Text] [Related]

  • 8. Determinations of 15N chemical shift anisotropy magnitudes in a uniformly 15N,13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy.
    Wylie BJ, Franks WT, Rienstra CM.
    J Phys Chem B; 2006 Jun 08; 110(22):10926-36. PubMed ID: 16771346
    [Abstract] [Full Text] [Related]

  • 9. Amino-acid selective experiments on uniformly 13C and 15N labeled proteins by MAS NMR: Filtering of lysines and arginines.
    Jehle S, Rehbein K, Diehl A, van Rossum BJ.
    J Magn Reson; 2006 Dec 08; 183(2):324-8. PubMed ID: 16990042
    [Abstract] [Full Text] [Related]

  • 10. Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
    Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ.
    J Biomol NMR; 2005 Apr 08; 31(4):279-93. PubMed ID: 15928995
    [Abstract] [Full Text] [Related]

  • 11. Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning.
    Fujiwara T, Todokoro Y, Yanagishita H, Tawarayama M, Kohno T, Wakamatsu K, Akutsu H.
    J Biomol NMR; 2004 Apr 08; 28(4):311-25. PubMed ID: 14872124
    [Abstract] [Full Text] [Related]

  • 12. Protein side-chain dynamics as observed by solution- and solid-state NMR spectroscopy: a similarity revealed.
    Agarwal V, Xue Y, Reif B, Skrynnikov NR.
    J Am Chem Soc; 2008 Dec 10; 130(49):16611-21. PubMed ID: 19049457
    [Abstract] [Full Text] [Related]

  • 13. Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
    Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM.
    J Am Chem Soc; 2005 Sep 07; 127(35):12291-305. PubMed ID: 16131207
    [Abstract] [Full Text] [Related]

  • 14. Experiments and strategies for the assignment of fully 13C/15N-labelled polypeptides by solid state NMR.
    Straus SK, Bremi T, Ernst RR.
    J Biomol NMR; 1998 Jul 07; 12(1):39-50. PubMed ID: 9729787
    [Abstract] [Full Text] [Related]

  • 15. Three-dimensional 13C shift/1H-15N coupling/15N shift solid-state NMR correlation spectroscopy.
    Gu Z, Opella SJ.
    J Magn Reson; 1999 Jun 07; 138(2):193-8. PubMed ID: 10341122
    [Abstract] [Full Text] [Related]

  • 16. Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.
    McDermott A, Polenova T, Bockmann A, Zilm KW, Paulson EK, Martin RW, Montelione GT.
    J Biomol NMR; 2000 Mar 07; 16(3):209-19. PubMed ID: 10805127
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  • 18. Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
    Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM.
    Biochemistry; 1990 Sep 04; 29(35):8172-84. PubMed ID: 2261471
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