Prediction of protein thermostability from their primary structure: the current state and development factors

   


1. Institute of Biomedical Chemistry, Moscow, Russia
Type: Review
DOI: 10.18097/PBMC20176302124      PubMed Id: 28414283
Year: 2017 vol: 63  issue:2  pages: 124-131
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.
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Reference: Grishin D.V., Pokrovskaya M.V., Podobed O.V., Gladilina Ju.A., Pokrovsky V.S., Aleksandrova S.S., Sokolov N.N., Prediction of protein thermostability from their primary structure: the current state and development factors, Biomeditsinskaya khimiya, 2017, vol: 63(2), 124-131.
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