文献类型：期刊文献

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

作者：Liu, Shucheng[1];Liu, Yuan[1];Luo, Shuai[1];Dong, Andi[1];Liu, Mengna[1];Ji, Hongwu[1];Gao, Jing[1];Hao, Jiming[1]

机构：[1]Guangdong Ocean Univ, Coll Food Sci & Technol, Guangdong Prov Key Lab Aquat Prod Proc & Safety, Guangdong Prov Seafood Engn Technol Res Ctr,Key L, Zhanjiang, Peoples R China

年份：2017

卷号：21

起止页码：270

外文期刊名：JOURNAL OF CO2 UTILIZATION

收录：SCI-EXPANDED(收录号：WOS:000411443200032)、、EI(收录号：20173204029926)、Scopus(收录号：2-s2.0-85026826980)、WOS

基金：This work was supported by the National Natural Science Foundation of China [31371801]; Project of Enhancing School With Innovation of Guangdong Ocean University [GDOU2017052603]; and Modern Agro-industry Technology Research System of China [CARS-47]; Science and Technology Planning Project of Guangdong [2015A020209158].

语种：英文

外文关键词：Dense-phase carbon dioxide; Myosin heavy chain; Conformation changes; Interaction; Molecular dynamics simulation

外文摘要：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.