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107 related items for PubMed ID: 22988852

  • 1. Residual dipolar couplings measured in unfolded proteins are sensitive to amino-acid-specific geometries as well as local conformational sampling.
    Huang JR, Gentner M, Vajpai N, Grzesiek S, Blackledge M.
    Biochem Soc Trans; 2012 Oct; 40(5):989-94. PubMed ID: 22988852
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. 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
    [Abstract] [Full Text] [Related]

  • 4. Residual dipolar couplings in short peptides reveal systematic conformational preferences of individual amino acids.
    Dames SA, Aregger R, Vajpai N, Bernado P, Blackledge M, Grzesiek S.
    J Am Chem Soc; 2006 Oct 18; 128(41):13508-14. PubMed ID: 17031964
    [Abstract] [Full Text] [Related]

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  • 6. 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
    [Abstract] [Full Text] [Related]

  • 7. Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings.
    Mohana-Borges R, Goto NK, Kroon GJ, Dyson HJ, Wright PE.
    J Mol Biol; 2004 Jul 23; 340(5):1131-42. PubMed ID: 15236972
    [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. 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
    [Abstract] [Full Text] [Related]

  • 10. Unfolded protein ensembles, folding trajectories, and refolding rate prediction.
    Das A, Sin BK, Mohazab AR, Plotkin SS.
    J Chem Phys; 2013 Sep 28; 139(12):121925. PubMed ID: 24089737
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. Residual dipolar couplings in short peptidic foldamers: combined analyses of backbone and side-chain conformations and evaluation of structure coordinates of rigid unnatural amino acids.
    Schmid MB, Fleischmann M, D'Elia V, Reiser O, Gronwald W, Gschwind RM.
    Chembiochem; 2009 Feb 13; 10(3):440-4. PubMed ID: 19156789
    [Abstract] [Full Text] [Related]

  • 13. 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
    [Abstract] [Full Text] [Related]

  • 14. Measurement and analysis of NMR residual dipolar couplings for the study of intrinsically disordered proteins.
    Salmon L, Jensen MR, Bernadó P, Blackledge M.
    Methods Mol Biol; 2012 Feb 03; 895():115-25. PubMed ID: 22760316
    [Abstract] [Full Text] [Related]

  • 15. Calculation of residual dipolar couplings from disordered state ensembles using local alignment.
    Marsh JA, Baker JM, Tollinger M, Forman-Kay JD.
    J Am Chem Soc; 2008 Jun 25; 130(25):7804-5. PubMed ID: 18512919
    [Abstract] [Full Text] [Related]

  • 16. Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.
    Schneider R, Huang JR, Yao M, Communie G, Ozenne V, Mollica L, Salmon L, Jensen MR, Blackledge M.
    Mol Biosyst; 2012 Jan 25; 8(1):58-68. PubMed ID: 21874206
    [Abstract] [Full Text] [Related]

  • 17. 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]

  • 18. 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
    [Abstract] [Full Text] [Related]

  • 19. Conformational distributions of unfolded polypeptides from novel NMR techniques.
    Meier S, Blackledge M, Grzesiek S.
    J Chem Phys; 2008 Feb 07; 128(5):052204. PubMed ID: 18266409
    [Abstract] [Full Text] [Related]

  • 20. Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins.
    Avbelj F.
    J Mol Biol; 2000 Jul 28; 300(5):1335-59. PubMed ID: 10903873
    [Abstract] [Full Text] [Related]

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