Zou Ling-Nan
Department of Chemistry, The Pennsylvania State University, University Park, PA 16801. USA.
bioRxiv. 2025 Mar 29:2025.03.26.645477. doi: 10.1101/2025.03.26.645477.
We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers.
我们描述了结构化随机结合（SRB），这是一种基于无序系统统计物理学的蛋白质-蛋白质相互作用的最小模型。在这个模型中，非特异性结合是随机蛋白质之间相互作用的普遍结果，表现出从高温状态到低温状态的相变，在高温状态下非特异性复合物是短暂的，缺乏明确的相互作用界面，而在低温状态下复合物结构被冻结，存在明确的相互作用界面。在数值上，弱结合的非特异性复合物可以演变成紧密结合的、高度特异性的复合物，但前提是沿着肽主链的结构相关长度较短；此外，进化出的紧密结合的同二聚体倾向于与真实蛋白质同二聚体中占主导地位的相同界面结构。
