亚基相互作用在成人血红蛋白构象转变中的作用：显式溶剂分子动力学研究
Role of the Subunits Interactions in the Conformational Transitions in Adult Human Hemoglobin: an Explicit Solvent Molecular Dynamics Study
摘要：
由于生理条件下配体结合位点、氨基酸残基和一些其他溶质之间的动态相互作用，血红蛋白在配体结合时表现出变构结构变化。本文用分子动力学研究了成人血红蛋白两个未连接的（脱氧）T结构和两个完全连接的（氧）R、R2结构的动力学和四级结构变化。结果表明，在亚微秒的时间尺度上，有没有明显的差异，在全球动态的氨基酸残基的氧和脱氧形式的个别结构。此外，R，R2相对稳定，在模拟的时间尺度内没有出现四级构象变化，而T结构动态上更灵活，表现出T \rightarrow R四级构象转变，这种转变是通过α1β2和α2β1界面残基的相对旋转传播的.
英文摘要：
Hemoglobin exhibits allosteric structural changes upon ligand binding due to the dynamic interactions between the ligand binding sites, the amino acids residues and some other solutes present under physiological conditions. In the present study, the dynamical and quaternary structural changes occurring in two unligated (deoxy-) T structures, and two fully ligated (oxy-) R, R2 structures of adult human hemoglobin were investigated with molecular dynamics. It is shown that, in the sub-microsecond time scale, there is no marked difference in the global dynamics of the amino acids residues in both the oxy- and the deoxy- forms of the individual structures. In addition, the R, R2 are relatively stable and do not present quaternary conformational changes within the time scale of our simulations while the T structure is dynamically more flexible and exhibited the T\rightarrow R quaternary conformational transition, which is propagated by the relative rotation of the residues at the α1β2 and α2β1 interface.
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