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.
  
• (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.