顺磁核磁共振技术研究蛋白质遭遇复合物的动态结构  

Investigation of Dynamic Structure of Protein Encountering Complex with Paramagnetic NMR

作　　者：赵昶 龚洲 ZHAO Chang;GONG Zhou(Innovation Academy for Precision Measurement Science and Technology,Chinese Academy of Sciences,Wuhan 430071,China;University of Chinese Academy of Sciences,Beijing 100049,China)

机构地区：[1]中国科学院精密测量科学与技术创新研究院,湖北武汉430071 [2]中国科学院大学,北京100049

出　　处：《波谱学杂志》2023年第2期148-157,共10页Chinese Journal of Magnetic Resonance

摘　　要：蛋白质依靠短程相互作用识别配体蛋白进而行使生物学功能,其相互作用界面仅占据蛋白质总表面积的一部分.因此,蛋白质与配体蛋白需要形成一系列遭遇复合物系综结构来减少构象搜索空间以加快结合速度.由于遭遇复合物在溶液体系中存在时间短、丰度低,因而很难被传统结构生物学技术捕捉到.本文选用组氨酸磷酸载体蛋白(HPr)和酶II(EIIAGlc)复合物为研究体系,采用顺磁弛豫增强(Paramagnetic Relaxation Enhancement,PRE)技术对遭遇复合物的系综结构及动力学性质进行表征,并用分子动力学模拟方法对实验结果进行验证,发现HPr在溶液体系中首先与EIIAGlc在3个方向上形成遭遇复合物,进而促进特异性复合物的形成.该方法不仅能够在溶液体系中观察遭遇复合物系综结构,还有望应用于生物大分子领域,揭示蛋白质在复杂生理网络中的相互作用机制及动力学行为.Proteins recognize partner proteins and take function through short-range interaction at a small interface area.Therefore,protein and its partner form a series of encounter complex ensembles on the pathway to simplify conformational searching and facilitate protein-protein association.The encounter complex is hard to detect by traditional structural-biology methods due to its short life and low population.This paper chose histidine phosphate carrier protein(HPr)and enzyme II(EIIAGlc)complex as the research target,combining paramagnetic relaxation enhancement(PRE)with molecular dynamics simulation to characterize the encounter complex structure and dynamics.We found that the HPr first formed encounter complexes with EIIAGlc in three directions,and then compelled the formation of the specific complex.The methods utilized in this paper can visualize the encounter complex ensembles,and help understand the mechanism of bio-molecule interaction and protein function pathway in cell.

关 键 词：核磁共振(NMR) 遭遇复合物 分子动力学模拟 糖磷酸转移酶系统 

分 类 号：O482.53[理学—固体物理]