Strategy for Stabilization of CutA1 Proteins Due to Ion–Ion Interactions at Temperatures of over 100 °C

• DOI: 10.1021/acs.biochem.8b00103
• Publication Date: 2018-04-12T17:34:06Z
• Authors: Yoshinori Matsuura; Michiyo Takehira; George I. Makhatadze; Yasumasa Joti; Hisashi Naitow; Naoki Kunishima; Katsuhide Yutani
• Keywords: Ions; 0303 health sciences; Hot Temperature; Protein Conformation; Escherichia coli Proteins; 3. Good health; 03 medical and health sciences; Enzyme Stability; Escherichia coli; Thermodynamics; Mutant Proteins; Amino Acid Sequence; Hydrophobic and Hydrophilic Interactions

In order to elucidate the contribution of charged residues protein stabilization at temperatures over 100 °C, we constructed many mutants CutA1 ( EcCutA1) from Escherichia coli. The goal was see if one can achieve same stability as for a hyperthermophile Pyrococcus horikoshii that has denaturation temperature near 150 °C. hydrophobic mutant EcCutA1 Ec0VV) with Td) 113.2 °C used template mutations. highest Td Ec0VV substituted by single residue 118.4 Multiple ion were also combination and found have an increased thermostability. multiple nine had 142.2 To evaluate energy ion-ion interactions proteins, structural ensemble obtained molecular dynamics simulation 300 K. ionic linearly increases increments computed proteins even up 140 suggesting cumulatively contribute high temperatures.