Molecular dynamics simulation of the interaction between dense-phase carbon dioxide and the myosin heavy chain

作者：Liu, Shucheng^*; Liu, Yuan; Luo, Shuai; Dong, Andi; Liu, Mengna; Ji, Hongwu; Gao, Jing; Hao, Jiming

来源：Journal of CO2 Utilization, 2017, 21: 270-279.

DOI：10.1016/j.jcou.2017.07.025

• Dense-phase carbon dioxide
• Myosin heavy chain
• Conformation changes
• Interaction
• Molecular dynamics simulation

Dense-phase carbon dioxide (DPCD) can induce myosin denaturation and aggregation and result in the formation of a gel. To explore the mechanism that DPCD induce myosin the formation of gels, molecular dynamics simulations were used to investigate the effects of DPCD on the structural properties of the myosin heavy chain (MHC, GenBank Accession No: BAM65721.1) from Litopenaeus vannamei. In addition, the interaction between the MHC and CO2 was explored under the coupling of pressure and temperature. To facilitate a better understanding and comparison, the structure of MHC was simulated in water at 0.1 MPa and 50 degrees C (called the myosin-water system, MWS) and in water and DPCD at 25 MPa and 50 degrees C (called the myosin-water-DPCD system, MWDS). The analysis of the root-mean-square deviation (RMSD) and root-mean-square fluctuation (RMSF) revealed that the conformation of the MHC in both MWDS and MWS changed significantly relative to its initial structure. Moreover, the results of the solvent-accessible surface area demonstrated that the MHC structure changes from a compact arrangement to a looser arrangement in both MWDS and MWS. Finally, the results from investigations into the secondary structures showed that the a-helix content of the MHC decreased, whereas the beta-turn and random coil content increased. Greater overall structural variations of the MHC were observed in MWDS than those observed in MWS. DPCD exerts a substantial effect on the MHC structure because of its hydrogen bonding, electrostatic repulsion and hydrophobic interactions with the MHC.

• 出版日期2017-10
• 单位广东海洋大学