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以一种基于目标蛋白凝血酶的取代反应来研究核酸适体与互补核酸和核酸适体与目标蛋白之间竞争结合的热力学特性,研究了核酸适体-互补核酸的解离反应和在目标蛋白存在下取代反应的平衡常数、标准焓变和标准熵变等热力学参数,结果表明该取代反应是一个熵驱动的自发过程,熵驱动从双链的核酸转变为核酸适体-目标蛋白的复合物.该热力学研究会对核酸适体-互补核酸和核酸适体-凝血酶之间的结合过程的机理有一个更深的理解,将有助于进一步揭示核酸与蛋白这两种生命中最关键物质之间的相互作用和关系,为更好地理解基本的生物过程和预测设计适体生物传感器,发展用于疾病诊断的方法有着重要的意义.
The thermodynamic properties of aptamer-complementary nucleic acid and aptamer-target protein were studied based on the substitution reaction of target protein thrombin. The dissociation reaction of aptamer-complementary nucleic acid and the target protein The results show that the substitution reaction is an entropy-driven spontaneous process, and entropy drives the transformation from double-stranded nucleic acid to aptamer-target protein complex The thermodynamic study will have a deeper understanding of the mechanistic aspects of the aptamer-complementary nucleic acid aptamer-thrombin binding process and will help further reveal the most critical of the two life-span nucleic acids and proteins It is of great importance to develop aptamer biosensors and to develop methods for disease diagnosis to better understand basic biological processes and predictions.