Böckmann A - Search Results

1

CONFINE-MAS: a magic-angle spinning NMR probe that confines the sample in case of a rotor explosion.

Wiegand T, Hunkeler A, Däpp A, Verasdonck J, Cadalbert R, Bousset L, Melki R, Böckmann A, Meier BH. Wiegand T, et al. Among authors: bockmann a. J Biomol NMR. 2018 Dec;72(3-4):171-177. doi: 10.1007/s10858-018-0218-x. Epub 2018 Dec 10. J Biomol NMR. 2018. PMID: 30536187

2

Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state.

McDermott A, Polenova T, Bockmann A, Zilm KW, Paulson EK, Martin RW, Montelione GT. McDermott A, et al. Among authors: bockmann a. J Biomol NMR. 2000 Mar;16(3):209-19. doi: 10.1023/a:1008391625633. J Biomol NMR. 2000. PMID: 10805127 Free article.

3

Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh.

Böckmann A, Lange A, Galinier A, Luca S, Giraud N, Juy M, Heise H, Montserret R, Penin F, Baldus M. Böckmann A, et al. J Biomol NMR. 2003 Dec;27(4):323-39. doi: 10.1023/a:1025820611009. J Biomol NMR. 2003. PMID: 14512730

4

NMR spectra of a microcrystalline protein at 30 kHz MAS.

Ernst M, Detken A, Böckmann A, Meier BH. Ernst M, et al. Among authors: bockmann a. J Am Chem Soc. 2003 Dec 24;125(51):15807-10. doi: 10.1021/ja0369966. J Am Chem Soc. 2003. PMID: 14677971

5

Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.

Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A. Böckmann A, et al. J Biomol NMR. 2005 Jul;32(3):195-207. doi: 10.1007/s10858-005-8073-y. J Biomol NMR. 2005. PMID: 16132820

6

Structural constraints for the Crh protein from solid-state NMR experiments.

Gardiennet C, Loquet A, Etzkorn M, Heise H, Baldus M, Böckmann A. Gardiennet C, et al. Among authors: bockmann a. J Biomol NMR. 2008 Apr;40(4):239-50. doi: 10.1007/s10858-008-9229-3. Epub 2008 Mar 5. J Biomol NMR. 2008. PMID: 18320329 Free PMC article.

7

Polarization transfer over the water-protein interface in solids.

Lesage A, Gardiennet C, Loquet A, Verel R, Pintacuda G, Emsley L, Meier BH, Böckmann A. Lesage A, et al. Among authors: bockmann a. Angew Chem Int Ed Engl. 2008;47(31):5851-4. doi: 10.1002/anie.200801110. Angew Chem Int Ed Engl. 2008. PMID: 18613186 No abstract available.

8

The molecular organization of the fungal prion HET-s in its amyloid form.

Wasmer C, Schütz A, Loquet A, Buhtz C, Greenwald J, Riek R, Böckmann A, Meier BH. Wasmer C, et al. Among authors: bockmann a. J Mol Biol. 2009 Nov 20;394(1):119-27. doi: 10.1016/j.jmb.2009.09.015. Epub 2009 Sep 11. J Mol Biol. 2009. PMID: 19748509

9

Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules.

Loquet A, Bousset L, Gardiennet C, Sourigues Y, Wasmer C, Habenstein B, Schütz A, Meier BH, Melki R, Böckmann A. Loquet A, et al. Among authors: bockmann a. J Mol Biol. 2009 Nov 20;394(1):108-18. doi: 10.1016/j.jmb.2009.09.016. Epub 2009 Sep 11. J Mol Biol. 2009. PMID: 19748512

10

Characterization of different water pools in solid-state NMR protein samples.

Böckmann A, Gardiennet C, Verel R, Hunkeler A, Loquet A, Pintacuda G, Emsley L, Meier BH, Lesage A. Böckmann A, et al. J Biomol NMR. 2009 Nov;45(3):319-27. doi: 10.1007/s10858-009-9374-3. J Biomol NMR. 2009. PMID: 19779834

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