ABSTRACT
Department of Biochemistry, Faculty of Natural Science, Charles University in Prague, Hlavova 8, 128 43 Prague 2, Czech Republic.
Emails: Helena.Ryslava@natur.cuni.cz * Corresponding author: Veronika.Doubnerova@natur.cuni.cz
All proteins can function correctly only in their native state; it means thermodynamically most stable conformation. In the cell, where the protein concentration is usually relatively high, it is important that newly synthesized proteins are correctly folded without misfolded intermediates and aggregates. The transport of the protein to appropriate compartment needs the protein to keep in enlarged form. All living cells have evolved systems, which assist in folding and transport of proteins synthesized de novo. These systems include molecular chaperons, designed also as heat shock proteins (HSPs), due to their enhanced amounts after exposure to elevated temperature. Increased temperature causes changes in threedimensional structure of proteins and denaturation; therefore the cell’s demands on molecular chaperons are quite enhanced (Frydman 2001; Hartl et al. 2011; Gething and Sambrook 1992). Furthermore also other types of stress such as cold, drought, high salt concentration, heavy metals, free radicals and UV light are associated with synthesis of heat shock proteins (Gupta and Tuteja 2011; Katschinski 2004).
