Molecular Peculiarities of Pro- and Eukaryotic Proteins Possessing Natural Adaptation to Low Temperatures
DOI:
https://doi.org/10.15407/cryo25.03.219Keywords:
cold adaptation, low temperatures, enzymes, structural proteins, amino acids, polarity, hydrophobicityAbstract
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
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