Protein piezophilicity: Solvent accessibility-based difference of amino acid in adaptation of proteins to high hydrostatic pressure

Abstract:

Abstract: [Objective] To investigate the structural distribution responsible for protein piezophilicity is of great significanceimportant for understanding the stability of piezophilic protein and would help to develop a practical strategy for designing piezophilic proteins. [Methods] We introduced a systematic comparative analysis of 43 pairs of piezophilic and non-piezophilic proteins. Three kinds of residue structural states such as external, intermediate and internal were considered for analyzing the structural patterns of single amino acids and amino acids in different groups. [Results] The statistical tests revealed that higher frequency in external state of Cys, Asp, Asn and Lys at the expense of Pro and Arg, higher frequency in intermediate state of Ile and Met at the expense of Trp, higher frequency in internal state of Cys and Ile at the expense of Ala, higher frequency in external and internal state of non-barophilic amino acids groups, lower frequency in external state of neutral and large amino acids groups could be critical factors related with protein piezophilicity. [Conclusion] The external state was the domain that had the most differences between piezophilic and non-piezophilic proteins, and it should be a hot spot for designing and engineering new piezophilic proteins. At the same time, the pressure asymmetry index should be revised based on more datasets.

Key words:Keywords: Piezophilic microbes; structure analysis; systematical analysis; solvent accessibility; piezophilic adaptation