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Journal Article (13)

  1. Journal Article
    Karpinar, P.; Gajula Balija, M. B.; Kügler, S.; Opazo, F.; Rezaei-Ghaleh, N.; Wender, N.; Kim, H. Y.; Taschenberger, G.; Falkenburger, B. H.; Heise, H. et al.; Kumar, A.; Riedel, D.; Fichtner, L.; Voigt, A.; Braus, G. H.; Giller, K.; Becker, S.; Herzig, A.; Baldus, M.; Jäckle, H.; Eimer, S.; Schulz, J. B.; Griesinger, C.; Zweckstetter, M.: Pre-fibrillar α-synuclein variants with impaired bold β-structure increase neurotoxicity in Parkinson's disease models. EMBO Journal 28 (20), pp. 3256 - 3268 (2009)
  2. Journal Article
    Heise, H.; Celej, M. S.; Becker, S.; Riedel, D.; Pelah, A.; Kumar, A.; Jovin, T. M.; Baldus, M.: Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant α-synuclein. Journal of Molecular Biology 380 (3), pp. 444 - 450 (2008)
  3. Journal Article
    Gardiennet, C.; Loquet, A.; Boeckmann, A.; Etzkorn, M.; Heise, H.; Baldus, M.: Structural constraints for the Crh protein from solid-state NMR experiments. Journal of Biomolecular NMR 40 (4), pp. 239 - 250 (2008)
  4. Journal Article
    Kim, H. Y.; Heise, H.; Fernandez, C. O.; Baldus, M.; Zweckstetter, M.: Correlation of amyloid fibril beta-structure with the unfolded state of alpha-synuclein. ChemBioChem 8 (14), pp. 1671 - 1674 (2007)
  5. Journal Article
    Heise, H.; Hoyer, W.; Becker, S.; Andronesi, O.; Riedel, D.; Baldus, M.: Moleculare-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studies by solid-state NMR. Proceedings of the National Academy of Sciences of the United States of America 102 (44), pp. 15871 - 15876 (2005)
  6. Journal Article
    Andronesi, O.; Becker, S.; Seidel, K.; Heise, H.; Young, H.S.; Baldus, M.: Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. Journal of the American Chemical Society 127 (37), pp. 12965 - 12974 (2005)
  7. Journal Article
    Heise, H.; Luca, S.; de Groot, B. L.; Grubmueller, H.; Baldus, M.: Probing conformational disorder in neurotensin by two-dimensional solid-state NMR and comparison to molecular dynamics simulations. Biophysical Journal 89 (3), pp. 2113 - 2120 (2005)
  8. Journal Article
    Seidel, K.; Etzkorn, M.; Heise, H.; Becker, S.; Baldus, M.: High-resolution solid-state NMR studies on uniformly [C-13,N-15]-labeled ubiquitin. ChemBioChem 6 (9), pp. 1638 - 1647 (2005)
  9. Journal Article
    Luca, S.; Heise, H.; Lange, A.; Baldus, M.: Investigation of ligand-receptor systems by high-resolution solid-state NMR: Recent progress and perspectives. Archiv der Pharmazie 336 (5-6), pp. 217 - 228 (2005)
  10. Journal Article
    Heise, H.; Seidel, K.; Etzkorn, M.; Becker, S.; Baldus, M.: 3D NMR spectroscopy for resonance assignment and structure elucidation of proteins under MAS: novel pulse schemes and sensitivity considerations. Journal of Magnetic Resonance 173 (1), pp. 64 - 74 (2005)
  11. Journal Article
    Seidel, K.; Lange, A.; Becker, S.; Hughes, C. E.; Heise, H.; Baldus, M.: Protein solid-state NMR resonance assignments from (C-13, C-13) correlation spectroscopy. Physical Chemistry Chemical Physics 6 (22), pp. 5090 - 5093 (2004)
  12. Journal Article
    Boeckmann, A.; Lange, A.; Galinier, A.; Luca, S.; Giraud, N.; Juy, M.; Heise, H.; Montserret, R.; Penin, F.; Baldus, M.: Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh. Journal of Biomolecular NMR 27 (4), pp. 323 - 339 (2003)
  13. Journal Article
    Luca, S.; Heise, H.; Baldus, M.: High-resolution solid-state NMR applied to polypeptides and membrane proteins. Accounts of Chemical Research 36 (11), pp. 858 - 865 (2003)
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