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181 related items for PubMed ID: 15535698
1. Probing molecular interfaces using 2D magic-angle-spinning NMR on protein mixtures with different uniform labeling. Etzkorn M, Böckmann A, Lange A, Baldus M. J Am Chem Soc; 2004 Nov 17; 126(45):14746-51. PubMed ID: 15535698 [Abstract] [Full Text] [Related]
2. 13C nuclear overhauser polarization-magic-angle spinning nuclear magnetic resonance spectroscopy in uniformly 13C-labeled solid proteins. Katoh E, Takegoshi K, Terao T. J Am Chem Soc; 2004 Mar 24; 126(11):3653-7. PubMed ID: 15025494 [Abstract] [Full Text] [Related]
3. Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation. Marulanda D, Tasayco ML, McDermott A, Cataldi M, Arriaran V, Polenova T. J Am Chem Soc; 2004 Dec 22; 126(50):16608-20. PubMed ID: 15600367 [Abstract] [Full Text] [Related]
4. 3D structure determination of the Crh protein from highly ambiguous solid-state NMR restraints. Loquet A, Bardiaux B, Gardiennet C, Blanchet C, Baldus M, Nilges M, Malliavin T, Böckmann A. J Am Chem Soc; 2008 Mar 19; 130(11):3579-89. PubMed ID: 18284240 [Abstract] [Full Text] [Related]
5. Quantitative analysis of backbone dynamics in a crystalline protein from nitrogen-15 spin-lattice relaxation. Giraud N, Blackledge M, Goldman M, Böckmann A, Lesage A, Penin F, Emsley L. J Am Chem Soc; 2005 Dec 28; 127(51):18190-201. PubMed ID: 16366572 [Abstract] [Full Text] [Related]
7. NMR spectra of a microcrystalline protein at 30 kHz MAS. Ernst M, Detken A, Böckmann A, Meier BH. J Am Chem Soc; 2003 Dec 24; 125(51):15807-10. PubMed ID: 14677971 [Abstract] [Full Text] [Related]
11. Probing heteronuclear (15)N-(17)O and (13)C-(17)O connectivities and proximities by solid-state NMR spectroscopy. Hung I, Uldry AC, Becker-Baldus J, Webber AL, Wong A, Smith ME, Joyce SA, Yates JR, Pickard CJ, Dupree R, Brown SP. J Am Chem Soc; 2009 Feb 11; 131(5):1820-34. PubMed ID: 19138069 [Abstract] [Full Text] [Related]