1. [Prediction of protein thermostability from their primary structure: the current state and development factors].
- Author
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Grishin DV, Pokrovskaya MV, Podobed OV, Gladilina JA, Pokrovsky VS, Aleksandrova SS, and Sokolov NN
- Subjects
- Amino Acid Sequence, Amino Acid Substitution, Animals, Archaea chemistry, Bacteria chemistry, Hot Temperature, Humans, Protein Stability, Protein Structure, Secondary, Protein Structure, Tertiary, Proteins ultrastructure, Thermodynamics, Algorithms, Amino Acids chemistry, Protein Engineering, Proteins chemistry
- Abstract
The construction of proteins and peptides with desired properties, including resistance to high temperatures, as well as optimization of their amino acid composition, is an important and complex task, which attracts much attention in various branches of the basic sciences, and also in biomedicine and biotechnology. This raises the question: what method is more relevant for the at the pilot stage of research in order to estimate the influence of the planned amino acid substitutions on the thermostability of the resultant protein construct? In this brief review we have classified existing basic practical and theoretical approaches used in studies and predicting the thermal stability of native and recombinant polypeptides. Particular attention has been paid to the predictive potential of statistical methods for studying the thermodynamic parameters of the primary protein structure and prospects of their use.
- Published
- 2017
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