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Journal Abstract Search


567 related items for PubMed ID: 16117513

  • 1. A general strategy for the assignment of aliphatic side-chain resonances of uniformly 13C,15N-labeled large proteins.
    Xu Y, Lin Z, Ho C, Yang D.
    J Am Chem Soc; 2005 Aug 31; 127(34):11920-1. PubMed ID: 16117513
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  • 3. General method for suppression of diagonal peaks in heteronuclear-edited NOESY spectroscopy.
    Wu J, Fan JS, Pascal SM, Yang D.
    J Am Chem Soc; 2004 Nov 24; 126(46):15018-9. PubMed ID: 15547985
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  • 4. G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination.
    Shen Y, Atreya HS, Liu G, Szyperski T.
    J Am Chem Soc; 2005 Jun 29; 127(25):9085-99. PubMed ID: 15969587
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  • 5. SCAssign: a sparky extension for the NMR resonance assignment of aliphatic side-chains of uniformly 13C,15N-labeled large proteins.
    Zhang L, Yang D.
    Bioinformatics; 2006 Nov 15; 22(22):2833-4. PubMed ID: 16966359
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  • 6. Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).
    Schuetz A, Wasmer C, Habenstein B, Verel R, Greenwald J, Riek R, Böckmann A, Meier BH.
    Chembiochem; 2010 Jul 26; 11(11):1543-51. PubMed ID: 20572250
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  • 7. 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 26; 194(2):289-94. PubMed ID: 18706838
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  • 8. Three-dimensional 13C shift/1H-15N coupling/15N shift solid-state NMR correlation spectroscopy.
    Gu Z, Opella SJ.
    J Magn Reson; 1999 Jun 26; 138(2):193-8. PubMed ID: 10341122
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  • 9. Amino-acid selective experiments on uniformly 13C and 15N labeled proteins by MAS NMR: Filtering of lysines and arginines.
    Jehle S, Rehbein K, Diehl A, van Rossum BJ.
    J Magn Reson; 2006 Dec 26; 183(2):324-8. PubMed ID: 16990042
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  • 10. Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
    Venters RA, Farmer BT, Fierke CA, Spicer LD.
    J Mol Biol; 1996 Dec 20; 264(5):1101-16. PubMed ID: 9000633
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  • 11. Sequence-specific assignments of methyl groups in high-molecular weight proteins.
    Yang D, Zheng Y, Liu D, Wyss DF.
    J Am Chem Soc; 2004 Mar 31; 126(12):3710-1. PubMed ID: 15038713
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  • 12. The 2D NMR experiments H(C)CO2 and HCCO2 for assignment and pH titration of carboxylate groups in uniformly 15N/13C-labeled proteins.
    Pellecchia M, Iwai H, Szyperski T, Wüthrich K.
    J Magn Reson; 1997 Jan 31; 124(1):274-8. PubMed ID: 9424317
    [No Abstract] [Full Text] [Related]

  • 13. NMR with 13C, 15N-doubly-labeled DNA: the Antennapedia homeodomain complex with a 14-mer DNA duplex.
    Fernández C, Szyperski T, Ono A, Iwai H, Tate S, Kainosho M, Wüthrich K.
    J Biomol NMR; 1998 Jul 31; 12(1):25-37. PubMed ID: 9729786
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  • 14. Determinations of 15N chemical shift anisotropy magnitudes in a uniformly 15N,13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy.
    Wylie BJ, Franks WT, Rienstra CM.
    J Phys Chem B; 2006 Jun 08; 110(22):10926-36. PubMed ID: 16771346
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  • 15. An efficient procedure for assignment of the proton, carbon and nitrogen resonances in 13C/15N labeled nucleic acids.
    Nikonowicz EP, Pardi A.
    J Mol Biol; 1993 Aug 20; 232(4):1141-56. PubMed ID: 8396648
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  • 16. Auto-induction medium for the production of [U-15N]- and [U-13C, U-15N]-labeled proteins for NMR screening and structure determination.
    Tyler RC, Sreenath HK, Singh S, Aceti DJ, Bingman CA, Markley JL, Fox BG.
    Protein Expr Purif; 2005 Apr 20; 40(2):268-78. PubMed ID: 15766868
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  • 17. Automated NMR assignment of protein side chain resonances using automated projection spectroscopy (APSY).
    Hiller S, Joss R, Wider G.
    J Am Chem Soc; 2008 Sep 10; 130(36):12073-9. PubMed ID: 18710239
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  • 20. Assignment of aliphatic side-chain 1HN/15N resonances in perdeuterated proteins.
    Farmer BT, Venters RA.
    J Biomol NMR; 1996 Jan 10; 7(1):59-71. PubMed ID: 8720832
    [Abstract] [Full Text] [Related]


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