摘要
采用分子动力学模拟的方法,计算并分析了黄粉虫抗冻蛋白吸附甲烷水合物过程中局部结构的变化。研究表明,水合物结合位点上4号苏氨酸Thr4在靠近甲烷水合物表面时,其位置会发生变化以适应水合物的笼状结构,通过取代甲烷分子与水合物表面结合,并促使其他苏氨酸靠近水合物,最终黄粉虫抗冻蛋白吸附在水合物上,抑制了冰固体生长。本研究结果对研发可降解的天然产物类水合物抑制剂具有参考意义。
Molecular dynamics simulation was used to calculate and analyze the local structural changes of the Tenebrio molitor antifreeze proteins during the adsorption process with methane hydrates.Studies have shown that when threonine 4 at the hydrate binding site is close to the surface of methane hydrate,its position will change to adapt to the cage structure of the hydrate.replace methane molecules and bind to the surface of the hydrate,and promote other threonines to be close to the hydrate,and finally the antifreeze protein of Mealworm is adsorbed on the hydrate.thus inhibiting the growth of ice solids.The results of this study have reference significance for the research and development of biodegradable natural product-based hydrate inhibitors.
作者
黄慧怡
张楠
刘俊杰
HUANG Huiyi;ZHANG Nan;LIU Junjie(School of Physical Science and Technology,Inner Mongolia University,Hohhot O10021,China)
出处
《内蒙古大学学报(自然科学版)》
CAS
2024年第1期46-53,共8页
Journal of Inner Mongolia University:Natural Science Edition
基金
国家自然科学基金项目(62062053)
内蒙古自然科学基金项目(2022QN03012,2020BS01004)。
关键词
抗冻蛋白
甲烷水合物
分子动力学模拟
水合物结合位点
antifreeze protein
methane hydrate
molecular dynamics simulation
hydrate binding surfacesite