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Journal Abstract Search


164 related items for PubMed ID: 19854082

  • 1. DNP enhanced frequency-selective TEDOR experiments in bacteriorhodopsin.
    Bajaj VS, Mak-Jurkauskas ML, Belenky M, Herzfeld J, Griffin RG.
    J Magn Reson; 2010 Jan; 202(1):9-13. PubMed ID: 19854082
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  • 2. 3D TEDOR NMR experiments for the simultaneous measurement of multiple carbon-nitrogen distances in uniformly (13)C,(15)N-labeled solids.
    Jaroniec CP, Filip C, Griffin RG.
    J Am Chem Soc; 2002 Sep 11; 124(36):10728-42. PubMed ID: 12207528
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  • 4. Measurement of dipolar couplings in a uniformly (13)C,(15)N-labeled membrane protein: distances between the Schiff base and aspartic acids in the active site of bacteriorhodopsin.
    Jaroniec CP, Lansing JC, Tounge BA, Belenky M, Herzfeld J, Griffin RG.
    J Am Chem Soc; 2001 Dec 26; 123(51):12929-30. PubMed ID: 11749563
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  • 6. Atomic resolution protein structure determination by three-dimensional transferred echo double resonance solid-state nuclear magnetic resonance spectroscopy.
    Nieuwkoop AJ, Wylie BJ, Franks WT, Shah GJ, Rienstra CM.
    J Chem Phys; 2009 Sep 07; 131(9):095101. PubMed ID: 19739873
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  • 8. A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR.
    Zhang Z, Li J, Chen Y, Xie H, Yang J.
    J Magn Reson; 2017 Dec 07; 285():79-85. PubMed ID: 29126001
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  • 10. Determination of methyl 13C-15N dipolar couplings in peptides and proteins by three-dimensional and four-dimensional magic-angle spinning solid-state NMR spectroscopy.
    Helmus JJ, Nadaud PS, Höfer N, Jaroniec CP.
    J Chem Phys; 2008 Feb 07; 128(5):052314. PubMed ID: 18266431
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  • 12. Dynamic aspects of extracellular loop region as a proton release pathway of bacteriorhodopsin studied by relaxation time measurements by solid state NMR.
    Kawamura I, Ohmine M, Tanabe J, Tuzi S, Saitô H, Naito A.
    Biochim Biophys Acta; 2007 Dec 07; 1768(12):3090-7. PubMed ID: 18036552
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  • 13. High-frequency dynamic nuclear polarization in MAS spectra of membrane and soluble proteins.
    Rosay M, Lansing JC, Haddad KC, Bachovchin WW, Herzfeld J, Temkin RJ, Griffin RG.
    J Am Chem Soc; 2003 Nov 12; 125(45):13626-7. PubMed ID: 14599177
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  • 17. Soft-triple resonance solid-state NMR experiments for assignments of U-13C, 15N labeled peptides and proteins.
    Astrof NS, Griffin RG.
    J Magn Reson; 2002 Nov 12; 158(1-2):157-63. PubMed ID: 12419681
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  • 18. Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state.
    Petkova AT, Baldus M, Belenky M, Hong M, Griffin RG, Herzfeld J.
    J Magn Reson; 2003 Jan 12; 160(1):1-12. PubMed ID: 12565042
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  • 19. Rapid measurement of long-range distances in proteins by multidimensional 13C-19F REDOR NMR under fast magic-angle spinning.
    Shcherbakov AA, Hong M.
    J Biomol NMR; 2018 May 12; 71(1):31-43. PubMed ID: 29785460
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  • 20. Spectroscopic labeling of A, S/T in the 1H-15N HSQC spectrum of uniformly (15N-13C) labeled proteins.
    Chugh J, Hosur RV.
    J Magn Reson; 2008 Oct 12; 194(2):289-94. PubMed ID: 18706838
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