The plasma membrane’s main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents.

质膜的主要成分，即磷脂和膜蛋白，已知以脂质-蛋白质功能域和超复合物的形式组织。没有已知的活性膜固有过程来建立膜组织。因此，必须考虑热波动的相互作用和膜介导的蛋白质相互作用的生物物理决定因素，以了解膜蛋白质组织。在这里，我们使用高速原子力显微镜和动力学和膜弹性理论来研究模型膜蛋白在受控脂质环境中的寡聚和组装行为。我们发现膜疏水性不匹配调节寡聚化和组装能量学，以及二维组织。