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The review covers the findings in molecular modifications of proteins in cold-adapted organisms. According to the current data such modifications are attained via amino acid residue substitutions in a protein molecule, reduction of hydrogen bonds and salt bridges, hydrophobicity decrease. The specified modifications augment the flexibility of macromolecules thereby providing their functionality. The role of molecule-to-molecule interactions in protein stabilisation and their functional state within low temperature range is discussed. Probl Cryobiol Cryomed 2015; 25(3):219-234

Molecular peculiarities of pro- and eukaryotic proteins possessing natural adaptation to low temperatures