Genomic and proteomic analysis bring to biomedical labs qualitatively new technologies, which enable the complex look to genes and gene-related products — proteins. In contrary to genes, which number is definitive for given living system, the number of protein species varied substantially according the immediate living conditions of the system studied. Moreover, most of the proteins have the function associated with the tertiary structure of their molecule, e.g. with the space orientation so called folding and intracellular compartment where are they located. In in vitro systems the process of folding is inefficient and only minority of synthesized molecules have correct shape. In vivo most molecules mustrapidly fold to proper tertiary conformation, otherwise unfolded and misfolded proteins would be degraded. The promotion of protein folding is most probably the chaperones and chaperonins role. These molecules create a family of conserved proteins found in all compartments of prokaryotic and eukaryotic cells. Moreover, in in vivo systems synthesized and folded proteins must occupy the proper intracellular niche to express their function.

Keywords: protein; GroEL