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570 related items for PubMed ID: 19748338

  • 1. 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]

  • 2. 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]

  • 3. 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]

  • 4. 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]

  • 5. 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 23; 17(8):952-60. PubMed ID: 20450486
    [Abstract] [Full Text] [Related]

  • 6. Residual dipolar couplings in protein structure determination.
    de Alba E, Tjandra N.
    Methods Mol Biol; 2004 Aug 23; 278():89-106. PubMed ID: 15317993
    [Abstract] [Full Text] [Related]

  • 7. 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]

  • 8. 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]

  • 9. 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 Dec 16; 895():115-25. PubMed ID: 22760316
    [Abstract] [Full Text] [Related]

  • 10. Sensitivity of NMR residual dipolar couplings to perturbations in folded and denatured staphylococcal nuclease.
    Sallum CO, Martel DM, Fournier RS, Matousek WM, Alexandrescu AT.
    Biochemistry; 2005 May 03; 44(17):6392-403. PubMed ID: 15850373
    [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 03; 23(3):426-35. PubMed ID: 23545493
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 13. Monitoring protein folding at atomic resolution.
    Kumar TK, Yu C.
    Acc Chem Res; 2004 Dec 29; 37(12):929-36. PubMed ID: 15609984
    [Abstract] [Full Text] [Related]

  • 14. Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding.
    Korzhnev DM, Kay LE.
    Acc Chem Res; 2008 Mar 29; 41(3):442-51. PubMed ID: 18275162
    [Abstract] [Full Text] [Related]

  • 15. Structural characterization of intrinsically disordered proteins by the combined use of NMR and SAXS.
    Sibille N, Bernadó P.
    Biochem Soc Trans; 2012 Oct 29; 40(5):955-62. PubMed ID: 22988847
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Limitations of induced folding in molecular recognition by intrinsically disordered proteins.
    Hazy E, Tompa P.
    Chemphyschem; 2009 Jul 13; 10(9-10):1415-9. PubMed ID: 19462392
    [Abstract] [Full Text] [Related]

  • 18. Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters.
    Kragelj J, Blackledge M, Jensen MR.
    Adv Exp Med Biol; 2015 Jul 13; 870():123-47. PubMed ID: 26387101
    [Abstract] [Full Text] [Related]

  • 19. Atomic-level characterization of disordered protein ensembles.
    Mittag T, Forman-Kay JD.
    Curr Opin Struct Biol; 2007 Feb 13; 17(1):3-14. PubMed ID: 17250999
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  • 20. 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]

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