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Journal Abstract Search

339 related items for PubMed ID: 19908838

  • 1. 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]

  • 2. Mapping the conformational landscape of urea-denatured ubiquitin using residual dipolar couplings.
    Meier S, Grzesiek S, Blackledge M.
    J Am Chem Soc; 2007 Aug 08; 129(31):9799-807. PubMed ID: 17636913
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  • 3. 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
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  • 7. Sequence-specific mapping of the interaction between urea and unfolded ubiquitin from ensemble analysis of NMR and small angle scattering data.
    Huang JR, Gabel F, Jensen MR, Grzesiek S, Blackledge M.
    J Am Chem Soc; 2012 Mar 07; 134(9):4429-36. PubMed ID: 22309138
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  • 9. Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.
    Jensen MR, Salmon L, Nodet G, Blackledge M.
    J Am Chem Soc; 2010 Feb 03; 132(4):1270-2. PubMed ID: 20063887
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  • 10. Mapping the potential energy landscape of intrinsically disordered proteins at amino acid resolution.
    Ozenne V, Schneider R, Yao M, Huang JR, Salmon L, Zweckstetter M, Jensen MR, Blackledge M.
    J Am Chem Soc; 2012 Sep 12; 134(36):15138-48. PubMed ID: 22901047
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  • 11. Atomic-level characterization of disordered protein ensembles.
    Mittag T, Forman-Kay JD.
    Curr Opin Struct Biol; 2007 Feb 12; 17(1):3-14. PubMed ID: 17250999
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  • 13. Quantitative modelfree analysis of urea binding to unfolded ubiquitin using a combination of small angle X-ray and neutron scattering.
    Gabel F, Jensen MR, Zaccaï G, Blackledge M.
    J Am Chem Soc; 2009 Jul 01; 131(25):8769-71. PubMed ID: 19505145
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  • 15. Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation.
    Mukrasch MD, Markwick P, Biernat J, Bergen Mv, Bernadó P, Griesinger C, Mandelkow E, Zweckstetter M, Blackledge M.
    J Am Chem Soc; 2007 Apr 25; 129(16):5235-43. PubMed ID: 17385861
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  • 16. Electrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin.
    Avbelj F, Grdadolnik SG.
    Protein Sci; 2007 Feb 25; 16(2):273-84. PubMed ID: 17242431
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  • 17. Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.
    Jensen MR, Markwick PR, Meier S, Griesinger C, Zweckstetter M, Grzesiek S, Bernadó P, Blackledge M.
    Structure; 2009 Sep 09; 17(9):1169-85. PubMed ID: 19748338
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  • 18. Structure and disorder in an unfolded state under nondenaturing conditions from ensemble models consistent with a large number of experimental restraints.
    Marsh JA, Forman-Kay JD.
    J Mol Biol; 2009 Aug 14; 391(2):359-74. PubMed ID: 19501099
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  • 19. 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
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  • 20. Nonrandom structure in the urea-unfolded Escherichia coli outer membrane protein X (OmpX).
    Tafer H, Hiller S, Hilty C, Fernández C, Wüthrich K.
    Biochemistry; 2004 Feb 03; 43(4):860-9. PubMed ID: 14744128
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