Articles dans des revues avec comité de lecture (247)
  1. 155. Ruysschaert, J. M., Goormaghtigh, E., Homblé, F., Andersson, M., Liepinsh, E., & Otting, G. (1998). Lipid membrane binding of NK-lysin. FEBS letters, 425(2), 341-344.
  2. 156. Raussens, V., De Jongh, H. H., Pézolet, M., Ruysschaert, J. M., & Goormaghtigh, E. (1998). Secondary structure of the intact H+,K+-ATPase and of its membrane-embedded region. An attenuated total reflection infrared spectroscopy, circular dichroism and Raman spectroscopy study. European journal of biochemistry / FEBS, 252(2), 261-267.
  3. 157. Sturgis, J., Roberts, M., & Goormaghtigh, E. (1998). Transmembrane helix stability: the effect of helix-helix interactions studied by Fourier transform infrared spectroscopy. Biophysical journal, 74(2 Pt 1), 988-994. doi:10.1016/S0006-3495(98)74022-6
  4. 158. De Jongh, H. H., Goormaghtigh, E., & Ruysschaert, J. M. (1997). Amide-proton exchange of water-soluble proteins of different structural classes studied at the submolecular level by infrared spectroscopy. Biochemistry, 36(44), 13603-13610. doi:10.1021/bi971337p
  5. 159. De Jongh, H. H., Goormaghtigh, E., & Ruysschaert, J. M. (1997). Monitoring structural stability of trypsin inhibitor at the submolecular level by amide-proton exchange using Fourier transform infrared spectroscopy: a test case for more general application. Biochemistry, 36(44), 13593-13602. doi:10.1021/bi971336x
  6. 160. Gasset, M., Laynez, J., Menéndez, M., Raussens, V., & Goormaghtigh, E. (1997). Structural domain organization of gastric H+,K+-ATPase and its rearrangement during the catalytic cycle. The Journal of biological chemistry, 272(3), 1608-1614.
  7. 161. Raussens, V., Ruysschaert, J. M., & Goormaghtigh, E. (1997). Fourier transform infrared spectroscopy study of the secondary structure of the gastric H+,K+-ATPase and of its membrane-associated proteolytic peptides. The Journal of biological chemistry, 272(1), 262-270.
  8. 162. Goormaghtigh, E., De Jongh, H. H., & Ruysschaert, J. M. (1996). Relevance of protein thin films prepared for attenuated total reflection fourier transform infrared spectroscopy: Significance of the pH. Applied spectroscopy, 50(12), 1519-1527.
  9. 163. De Jongh, H. H., Goormaghtigh, E., & Ruysschaert, J. M. (1996). The different molar absorptivities of the secondary structure types in the amide I region: an attenuated total reflection infrared study on globular proteins. Analytical biochemistry, 242(1), 95-103. doi:10.1006/abio.1996.0434
  10. 164. Sonveaux, N., Shapiro, A., Goormaghtigh, E., Ling, V., & Ruysschaert, J. M. (1996). Secondary and tertiary structure changes of reconstituted P-glycoprotein. A Fourier transform attenuated total reflection infrared spectroscopy analysis. The Journal of biological chemistry, 271(40), 24617-24624.
  11. 165. Raussens, V., Narayanaswami, V., Goormaghtigh, E., Ryan, R. O., & Ruysschaert, J. M. (1996). Hydrogen/deuterium exchange kinetics of apolipophorin-III in lipid-free and phospholipid-bound states. An analysis by Fourier transform infrared spectroscopy. The Journal of biological chemistry, 271(38), 23089-23095.
  12. 166. Leenhouts, J. M., Török, Z., Mandieau, V., Goormaghtigh, E., & de Kruijff, B. (1996). The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes. Consequences for the action of a transmembrane potential. FEBS letters, 388(1), 34-38.
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