Clementi C, Carloni P, Maritan A
International School for Advanced Studies (SISSA) and Istituto Nazionale di Fisica della Materia, Via Beirut 2-4, 34014 Trieste, Italy.
Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9616-21. doi: 10.1073/pnas.96.17.9616.
Fundamental questions about role of the quaternary structures are addressed by using a statistical mechanics off-lattice model of a dimer protein. The model, in spite of its simplicity, captures key features of the monomer-monomer interactions revealed by atomic force experiments. Force curves during association and dissociation processes are characterized by sudden jumps followed by smooth behavior and form hysteresis loops. Furthermore, the process is reversible in a finite range of temperature stabilizing the dimer, and the width of the hysteresis loop increases as the design procedure improves: i.e., stabilizes the dimer more. It is shown that, in the interface between the two monomeric subunits, the design procedure naturally favors those amino acids whose mutual interaction is stronger.
通过使用二聚体蛋白质的统计力学非晶格模型，探讨了关于四级结构作用的基本问题。该模型尽管简单，却捕捉到了原子力实验揭示的单体-单体相互作用的关键特征。缔合和解离过程中的力曲线特征是突然跳跃，随后是平滑行为，并形成滞后回线。此外，该过程在使二聚体稳定的有限温度范围内是可逆的，并且滞后回线的宽度随着设计过程的改进而增加，即对二聚体的稳定作用更强。结果表明，在两个单体亚基之间的界面处，设计过程自然有利于那些相互作用更强的氨基酸。
