Characterization of rare conformational states of proteins by combination of high-pressure X-ray crystallography with high-pressure NMR spectroscopy. Application to the small Gprotein Ras, its oncogenic mutants and its drug complexes.

• Applicant: Professor Dr. Hans Robert Kalbitzer
• Subject Area: Structural Biology ; Biophysics
• Term: from 2017 to 2021
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 390275479

• Final Report Year: 2021

Final Report Abstract

No abstract available

Publications

• (2018) Conformational Transitions of the Ras Protein Involved in Macromolecular Interactions and Modulated by Small Compounds. A Biophysical Approach Using NMR and X-Ray Crystallography at Ambient and High Pressures. Doctoral thesis University of Regensburg
  Lopes, P.
  
• (2019) The pressure and temperature perturbation approach reveals a whole variety of conformational substates of amyloidogenic hIAPP monitored by 2D NMR spectroscopy. Biophys. Chem. 254, 106239
  Beck Erlach, M., Kalbitzer, H. R., Winter, R., Kremer, W.
  (See online at https://doi.org/10.1016/j.bpc.2019.106239)
• (2020) Pressure Dependence of Side Chain 1H and 15N-Chemical Shifts in the Model Peptides Ac-Gly-Gly-Xxx-Ala-NH2. J. Biomol. NMR 74, 381-399
  Beck Erlach, M., Koehler, J., Munte, C.E., Kremer, W., Crusca Jr, E., Kainosho, M., Kalbitzer, H. R.
  (See online at https://doi.org/10.1007/s10858-020-00326-w)