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380 related items for PubMed ID: 19021570

  • 1. Residual dipolar couplings as a tool to study molecular recognition of ubiquitin.
    Lakomek NA, Lange OF, Walter KF, Farès C, Egger D, Lunkenheimer P, Meiler J, Grubmüller H, Becker S, de Groot BL, Griesinger C.
    Biochem Soc Trans; 2008 Dec; 36(Pt 6):1433-7. PubMed ID: 19021570
    [Abstract] [Full Text] [Related]

  • 2. Analysis of interdomain dynamics in a two-domain protein using residual dipolar couplings together with 15N relaxation data.
    Ryabov Y, Fushman D.
    Magn Reson Chem; 2006 Jul; 44 Spec No():S143-51. PubMed ID: 16823894
    [Abstract] [Full Text] [Related]

  • 3. Various strategies of using residual dipolar couplings in NMR-driven protein docking: application to Lys48-linked di-ubiquitin and validation against 15N-relaxation data.
    van Dijk AD, Fushman D, Bonvin AM.
    Proteins; 2005 Aug 15; 60(3):367-81. PubMed ID: 15937902
    [Abstract] [Full Text] [Related]

  • 4. Theoretical analysis of residual dipolar coupling patterns in regular secondary structures of proteins.
    Mascioni A, Veglia G.
    J Am Chem Soc; 2003 Oct 15; 125(41):12520-6. PubMed ID: 14531696
    [Abstract] [Full Text] [Related]

  • 5. Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin.
    Salmon L, Bouvignies G, Markwick P, Lakomek N, Showalter S, Li DW, Walter K, Griesinger C, Brüschweiler R, Blackledge M.
    Angew Chem Int Ed Engl; 2009 Oct 15; 48(23):4154-7. PubMed ID: 19415702
    [Abstract] [Full Text] [Related]

  • 6. Self-consistency analysis of dipolar couplings in multiple alignments of ubiquitin.
    Hus JC, Peti W, Griesinger C, Brüschweiler R.
    J Am Chem Soc; 2003 May 14; 125(19):5596-7. PubMed ID: 12733874
    [Abstract] [Full Text] [Related]

  • 7. De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy.
    Briggman KB, Tolman JR.
    J Am Chem Soc; 2003 Aug 27; 125(34):10164-5. PubMed ID: 12926926
    [Abstract] [Full Text] [Related]

  • 8. Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings.
    Vajpai N, Gentner M, Huang JR, Blackledge M, Grzesiek S.
    J Am Chem Soc; 2010 Mar 10; 132(9):3196-203. PubMed ID: 20155903
    [Abstract] [Full Text] [Related]

  • 9. Ensemble calculations of unstructured proteins constrained by RDC and PRE data: a case study of urea-denatured ubiquitin.
    Huang JR, Grzesiek S.
    J Am Chem Soc; 2010 Jan 20; 132(2):694-705. PubMed ID: 20000836
    [Abstract] [Full Text] [Related]

  • 10. How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
    Clore GM, Schwieters CD.
    J Am Chem Soc; 2004 Mar 10; 126(9):2923-38. PubMed ID: 14995210
    [Abstract] [Full Text] [Related]

  • 11. Measurements of side-chain 13C-13C residual dipolar couplings in uniformly deuterated proteins.
    Vögeli B, Kovacs H, Pervushin K.
    J Am Chem Soc; 2004 Mar 03; 126(8):2414-20. PubMed ID: 14982448
    [Abstract] [Full Text] [Related]

  • 12. Refinement of ensembles describing unstructured proteins using NMR residual dipolar couplings.
    Esteban-Martín S, Fenwick RB, Salvatella X.
    J Am Chem Soc; 2010 Apr 07; 132(13):4626-32. PubMed ID: 20222664
    [Abstract] [Full Text] [Related]

  • 13. Projection angle restraints for studying structure and dynamics of biomolecules.
    Griesinger C, Peti W, Meiler J, Brüschweiler R.
    Methods Mol Biol; 2004 Apr 07; 278():107-21. PubMed ID: 15317994
    [Abstract] [Full Text] [Related]

  • 14. Conformational flexibility of a microcrystalline globular protein: order parameters by solid-state NMR spectroscopy.
    Lorieau JL, McDermott AE.
    J Am Chem Soc; 2006 Sep 06; 128(35):11505-12. PubMed ID: 16939274
    [Abstract] [Full Text] [Related]

  • 15. Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings.
    Bouvignies G, Markwick P, Brüschweiler R, Blackledge M.
    J Am Chem Soc; 2006 Nov 29; 128(47):15100-1. PubMed ID: 17117856
    [Abstract] [Full Text] [Related]

  • 16. Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings.
    Wöhnert J, Franz KJ, Nitz M, Imperiali B, Schwalbe H.
    J Am Chem Soc; 2003 Nov 05; 125(44):13338-9. PubMed ID: 14583012
    [Abstract] [Full Text] [Related]

  • 17. Exclusively heteronuclear NMR experiments to obtain structural and dynamic information on proteins.
    Bermel W, Bertini I, Felli IC, Peruzzini R, Pierattelli R.
    Chemphyschem; 2010 Feb 22; 11(3):689-95. PubMed ID: 20077554
    [Abstract] [Full Text] [Related]

  • 18. Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution.
    Lange OF, Lakomek NA, Farès C, Schröder GF, Walter KF, Becker S, Meiler J, Grubmüller H, Griesinger C, de Groot BL.
    Science; 2008 Jun 13; 320(5882):1471-5. PubMed ID: 18556554
    [Abstract] [Full Text] [Related]

  • 19. Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings.
    Nodet G, Salmon L, Ozenne V, Meier S, Jensen MR, Blackledge M.
    J Am Chem Soc; 2009 Dec 16; 131(49):17908-18. PubMed ID: 19908838
    [Abstract] [Full Text] [Related]

  • 20. Simultaneous measurement of protein one-bond residual dipolar couplings without increased resonance overlap.
    Vijayan V, Zweckstetter M.
    J Magn Reson; 2005 Jun 16; 174(2):245-53. PubMed ID: 15862241
    [Abstract] [Full Text] [Related]

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