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Project information
Proteins in metabolism and interaction of organisms with the environment

Information

This project doesn't include Faculty of Education. It includes Faculty of Science. Official project website can be found on muni.cz.
Project Identification
MSM0021622413
Project Period
1/2005 - 12/2011
Investor / Pogramme / Project type
Ministry of Education, Youth and Sports of the CR
  • Research Intents
MU Faculty or unit
Faculty of Science
  • prof. RNDr. Jaroslav Koča, DrSc.
Other MU Faculty/Unit
Central European Institute of Technology
Keywords
proteins, structure function relationships, protein complexes, proteome, metabolome

The proposal is the follow up of the previous, in our view successful, long-term research plan "Structure-Function Relationships of Biomolecules and their Role in Metabolism" studied in 1998-2004, and partly the project "Laboratory of Structure and Dynamics of Biomolecules" in the framework of program "250" studied in 1996-2000. The results of these projects were published in tens of scientific articles communicated in renowned international journals with high impact factors. The key aim was identification and characterization of low molecular weight substances involved in metabolism of bacteria and fungi with the special attention devoted to biochemical activities and the structure.
This new proposal will deal with other proteins from various organisms, for example animal proteins binding pheromones or proteins interacting with sacharides. The function and regulation of enzymes will be studied by novel methods suitable for monitoring of in vivo activity via monitoring of intracellular metabolites. We will continue to use structural methods. Keywords of the long-term research plan are protein, its function, structure, structure-function relationships and complexes of proteins. More general keywords are proteome and metabolome. The project will focus on such hot topics of current life sciences like protein/DNA interactions, synthesis of proteins on ribosome or applications of photo-labile groups for directed geometrical changes of protein-substrate complexes and regulation of enzymatic reactions.


Publications

Total number of publications: 836

2012

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