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Journal Abstract Search
218 related items for PubMed ID: 8995843
1. HCN, a triple-resonance NMR technique for selective observation of histidine and tryptophan side chains in 13C/15N-labeled proteins. Sudmeier JL, Ash EL, Günther UL, Luo X, Bullock PA, Bachovchin WW. J Magn Reson B; 1996 Dec; 113(3):236-47. PubMed ID: 8995843 [Abstract] [Full Text] [Related]
2. Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy. Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM. Biochemistry; 1990 Sep 04; 29(35):8172-84. PubMed ID: 2261471 [Abstract] [Full Text] [Related]
3. Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues. Löhr F, Rogov VV, Shi M, Bernhard F, Dötsch V. J Biomol NMR; 2005 Aug 04; 32(4):309-28. PubMed ID: 16211484 [Abstract] [Full Text] [Related]
4. Sequence-specific assignment of histidine and tryptophan ring 1H, 13C and 15N resonances in 13C/15N- and 2H/13C/15N-labelled proteins. Löhr F, Katsemi V, Betz M, Hartleib J, Rüterjans H. J Biomol NMR; 2002 Feb 04; 22(2):153-64. PubMed ID: 11883776 [Abstract] [Full Text] [Related]
5. Two-dimensional NMR studies of staphylococcal nuclease: evidence for conformational heterogeneity from hydrogen-1, carbon-13, and nitrogen-15 spin system assignments of the aromatic amino acids in the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex. Wang JF, Hinck AP, Loh SN, Markley JL. Biochemistry; 1990 May 01; 29(17):4242-53. PubMed ID: 2361141 [Abstract] [Full Text] [Related]
10. 3D triple-resonance NMR techniques for the sequential assignment of NH and 15N resonances in 15N- and 13C-labelled proteins. Weisemann R, Rüterjans H, Bermel W. J Biomol NMR; 1993 Jan 01; 3(1):113-20. PubMed ID: 8448431 [Abstract] [Full Text] [Related]
12. Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated IIIGlc, a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques. Pelton JG, Torchia DA, Meadow ND, Roseman S. Protein Sci; 1993 Apr 01; 2(4):543-58. PubMed ID: 8518729 [Abstract] [Full Text] [Related]
14. 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 01; 1768(12):3090-7. PubMed ID: 18036552 [Abstract] [Full Text] [Related]