谷蛋白
机制(生物学)
分子动力学
球蛋白
化学
生物系统
贮藏蛋白
计算生物学
生物化学
计算化学
生物
物理
基因
量子力学
免疫学
作者
Pengyu Zhu,Chunmin Ma,Yang Yang,Xin Bian,Likun Ren,Bing Wang,Xiaofei Liu,Fenglian Chen,Guang Zhang,Na Zhang
标识
DOI:10.1016/j.foodchem.2024.138615
摘要
Rice gluten, as the hydrophobic protein, exhibits restricted application value in hydrophilic food, which may be enhanced through interaction with soybean 11S globulin, characterized by favorable functional properties. This study aims at revealing their interaction mechanism via multi-spectroscopy and molecular dynamics simulation. The formation and structural change of rice glutelin-soybean 11S globulin complexes were detected using fluorescence, ultra–violet and circular dichroism spectra. The addition of 11S globulin increased the contents of α-helix, β-turn and random coil, but decreased β-sheet content, and the change in secondary structure was correlated with particle size. Moreover, exposure of hydrophobic groups and formation of disulfide bonds occurred in the complexes. Molecular dynamics simulation verified these experimental results through analyses of root mean square deviation and fluctuation, hydrogen bond, secondary structure, and binding free energy analysis. This study contributes to expounding the interaction mechanism of protein and protein from the molecular level.
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