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340 related items for PubMed ID: 21058670

  • 1. Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r).
    Otten R, Villali J, Kern D, Mulder FA.
    J Am Chem Soc; 2010 Dec 01; 132(47):17004-14. PubMed ID: 21058670
    [Abstract] [Full Text] [Related]

  • 2. A methyl-TROSY based 13C relaxation dispersion NMR experiment for studies of chemical exchange in proteins.
    Tugarinov V, Baber JL, Clore GM.
    J Biomol NMR; 2023 Jun 01; 77(3):83-91. PubMed ID: 37095392
    [Abstract] [Full Text] [Related]

  • 3. Quantifying millisecond exchange dynamics in proteins by CPMG relaxation dispersion NMR using side-chain 1H probes.
    Hansen AL, Lundström P, Velyvis A, Kay LE.
    J Am Chem Soc; 2012 Feb 15; 134(6):3178-89. PubMed ID: 22300166
    [Abstract] [Full Text] [Related]

  • 4. A (15)N CPMG relaxation dispersion experiment more resistant to resonance offset and pulse imperfection.
    Jiang B, Yu B, Zhang X, Liu M, Yang D.
    J Magn Reson; 2015 Aug 15; 257():1-7. PubMed ID: 26037134
    [Abstract] [Full Text] [Related]

  • 5. Characterization of enzyme motions by solution NMR relaxation dispersion.
    Loria JP, Berlow RB, Watt ED.
    Acc Chem Res; 2008 Feb 15; 41(2):214-21. PubMed ID: 18281945
    [Abstract] [Full Text] [Related]

  • 6. Revisiting 1HN CPMG relaxation dispersion experiments: a simple modification can eliminate large artifacts.
    Yuwen T, Kay LE.
    J Biomol NMR; 2019 Nov 15; 73(10-11):641-650. PubMed ID: 31646421
    [Abstract] [Full Text] [Related]

  • 7. The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy.
    Korzhnev DM, Religa TL, Lundström P, Fersht AR, Kay LE.
    J Mol Biol; 2007 Sep 14; 372(2):497-512. PubMed ID: 17689561
    [Abstract] [Full Text] [Related]

  • 8. Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach.
    Ishima R, Torchia DA.
    J Biomol NMR; 2003 Mar 14; 25(3):243-8. PubMed ID: 12652136
    [Abstract] [Full Text] [Related]

  • 9. Slow internal dynamics in proteins: application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme.
    Mulder FA, Hon B, Mittermaier A, Dahlquist FW, Kay LE.
    J Am Chem Soc; 2002 Feb 20; 124(7):1443-51. PubMed ID: 11841314
    [Abstract] [Full Text] [Related]

  • 10. A "Steady-State" Relaxation Dispersion Nuclear Magnetic Resonance Experiment for Studies of Chemical Exchange in Degenerate 1H Transitions of Methyl Groups.
    Tugarinov V, Okuno Y, Torricella F, Karamanos TK, Clore GM.
    J Phys Chem Lett; 2022 Dec 08; 13(48):11271-11279. PubMed ID: 36449372
    [Abstract] [Full Text] [Related]

  • 11. Quantitative measurement of exchange dynamics in proteins via (13)C relaxation dispersion of (13)CHD2-labeled samples.
    Rennella E, Schuetz AK, Kay LE.
    J Biomol NMR; 2016 Jun 08; 65(2):59-64. PubMed ID: 27251650
    [Abstract] [Full Text] [Related]

  • 12. Probing the Broad Time Scale and Heterogeneous Conformational Dynamics in the Catalytic Core of the Arf-GAP ASAP1 via Methyl Adiabatic Relaxation Dispersion.
    Chao FA, Li Y, Zhang Y, Byrd RA.
    J Am Chem Soc; 2019 Jul 31; 141(30):11881-11891. PubMed ID: 31293161
    [Abstract] [Full Text] [Related]

  • 13. Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.
    Orekhov VYu, Pervushin KV, Arseniev AS.
    Eur J Biochem; 1994 Feb 01; 219(3):887-96. PubMed ID: 8112340
    [Abstract] [Full Text] [Related]

  • 14. Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding.
    Tugarinov V.
    Prog Nucl Magn Reson Spectrosc; 2014 Feb 01; 77():49-68. PubMed ID: 24411830
    [Abstract] [Full Text] [Related]

  • 15. Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data.
    Xue Y, Ward JM, Yuwen T, Podkorytov IS, Skrynnikov NR.
    J Am Chem Soc; 2012 Feb 08; 134(5):2555-62. PubMed ID: 22206299
    [Abstract] [Full Text] [Related]

  • 16. Removal of slow-pulsing artifacts in in-phase 15N relaxation dispersion experiments using broadband 1H decoupling.
    Chatterjee SD, Ubbink M, van Ingen H.
    J Biomol NMR; 2018 Jun 08; 71(2):69-77. PubMed ID: 29860650
    [Abstract] [Full Text] [Related]

  • 17. Relaxation dispersion NMR spectroscopy for the study of protein allostery.
    Farber PJ, Mittermaier A.
    Biophys Rev; 2015 Jun 08; 7(2):191-200. PubMed ID: 28510170
    [Abstract] [Full Text] [Related]

  • 18. An improved 15N relaxation dispersion experiment for the measurement of millisecond time-scale dynamics in proteins.
    Hansen DF, Vallurupalli P, Kay LE.
    J Phys Chem B; 2008 May 15; 112(19):5898-904. PubMed ID: 18001083
    [Abstract] [Full Text] [Related]

  • 19. Histidine side-chain dynamics and protonation monitored by 13C CPMG NMR relaxation dispersion.
    Hass MA, Yilmaz A, Christensen HE, Led JJ.
    J Biomol NMR; 2009 Aug 15; 44(4):225-33. PubMed ID: 19533375
    [Abstract] [Full Text] [Related]

  • 20. Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.
    Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P.
    J Am Chem Soc; 2012 Sep 12; 134(36):14800-7. PubMed ID: 22908968
    [Abstract] [Full Text] [Related]

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