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205 related items for PubMed ID: 22901047

  • 1. 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]

  • 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. 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 16; 40(5):989-94. PubMed ID: 22988852
    [Abstract] [Full Text] [Related]

  • 4. 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]

  • 5. 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 Sep 09; 895():115-25. PubMed ID: 22760316
    [Abstract] [Full Text] [Related]

  • 6. Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.
    Kragelj J, Ozenne V, Blackledge M, Jensen MR.
    Chemphyschem; 2013 Sep 16; 14(13):3034-45. PubMed ID: 23794453
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein.
    Jensen MR, Houben K, Lescop E, Blanchard L, Ruigrok RW, Blackledge M.
    J Am Chem Soc; 2008 Jun 25; 130(25):8055-61. PubMed ID: 18507376
    [Abstract] [Full Text] [Related]

  • 9. A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.
    Rozentur-Shkop E, Goobes G, Chill JH.
    J Biomol NMR; 2016 Dec 25; 66(4):243-257. PubMed ID: 27844185
    [Abstract] [Full Text] [Related]

  • 10. 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]

  • 11. Describing intrinsically disordered proteins at atomic resolution by NMR.
    Jensen MR, Ruigrok RW, Blackledge M.
    Curr Opin Struct Biol; 2013 Jun 25; 23(3):426-35. PubMed ID: 23545493
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 13. 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]

  • 14. Compaction and binding properties of the intrinsically disordered C-terminal domain of Henipavirus nucleoprotein as unveiled by deletion studies.
    Blocquel D, Habchi J, Gruet A, Blangy S, Longhi S.
    Mol Biosyst; 2012 Jan 25; 8(1):392-410. PubMed ID: 22108848
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation.
    Abyzov A, Salvi N, Schneider R, Maurin D, Ruigrok RW, Jensen MR, Blackledge M.
    J Am Chem Soc; 2016 May 18; 138(19):6240-51. PubMed ID: 27112095
    [Abstract] [Full Text] [Related]

  • 17. Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters.
    Kragelj J, Blackledge M, Jensen MR.
    Adv Exp Med Biol; 2015 May 18; 870():123-47. PubMed ID: 26387101
    [Abstract] [Full Text] [Related]

  • 18. Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition.
    Jensen MR, Bernadó P, Houben K, Blanchard L, Marion D, Ruigrok RW, Blackledge M.
    Protein Pept Lett; 2010 Aug 18; 17(8):952-60. PubMed ID: 20450486
    [Abstract] [Full Text] [Related]

  • 19. Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.
    Rezaei-Ghaleh N, Blackledge M, Zweckstetter M.
    Chembiochem; 2012 May 07; 13(7):930-50. PubMed ID: 22505141
    [Abstract] [Full Text] [Related]

  • 20. Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.
    Sibille N, Bernadó P.
    Biochem Soc Trans; 2012 Oct 07; 40(5):955-62. PubMed ID: 22988847
    [Abstract] [Full Text] [Related]

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