11th BIOCEV-Krč Methodological Seminar

  • Date & Time: 7. 9. 2020  |  15:00
  • Location: Lecture hall of the Institute of Physiology

Topic: “Centre of Molecular Structure”


 

Topic: “Centre of Molecular Structure”

 

The following speakers will present at the seminar:

Jan Dohnálek, Ph.D.
Institute of Biotechnology of the Czech Academy of Sciences, Centre of Molecular Structure

“Invitation to perform your research at the Centre of Molecular Structure”
CMS offers open access to methods of molecular biophysics, macromolecular crystallization, diffraction, SAXS, structural mass spectrometry and time-resolved spectroscopy.

Jan Stránský, Ph.D.
Institute of Biotechnology of the Czech Academy of Sciences, Centre of Molecular Structure

“Macromolecular particle characterization using advanced SAXS”
Small angle X-ray scattering (SAXS) allows structural characterization of proteins, nucleic acids and other biological particles in solution. The state-of-art laboratory instrument in CMS brings possibilities for advanced experiments, for example coupling with chromatography system (SEC-SAXS) or in-situ UV-Vis spectroscopy.

Petr Pompach, Ph.D.
Institute of Biotechnology of the Czech Academy of Sciences, Centre of Molecular Structure

“Structural Mass Spectrometry – An Advanced Tool in Protein Structure Analysis””
Structural mass spectrometry is a fast growing field on analytical chemistry representing a new approach for protein structural studies. In CMS, the tools of structural mass spectrometry, including hydrogen-deuterium exchange or chemical cross-linking, are well established and allow to look beyond the edge of traditional structural techniques.

Prof. Tomáš Obšil, Ph.D. 
Faculty of Science, Charles University

CMS user talk

“Structural studies of interactions between calcium/calmodulin-dependent protein kinase kinase 2 (CaMKK2) and its binding partners calmodulin and 14-3-3 protein” 
This talk will summarize our recent effort in characterizing protein-protein interactions between CaMKK2 and its two regulatory binding partners calmodulin and the 14-3-3 protein using various biophysical approaches.

 

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