Physicochemical code for quinary protein interactions in Escherichia coli.

摘要: How proteins sense and navigate the cellular interior to find their functional partners remains poorly understood. An intriguing aspect of this search is that it relies on diffusive encounters with crowded background, made up protein surfaces are largely nonconserved. The question then if/how amenable selection biological control. To shed light issue, we examined motions three evolutionary divergent in Escherichia coli cytoplasm by in-cell NMR. results show motions, after all, follow simplistic physical-chemical rules: reveal a common dependence (i) net charge density, (ii) surface hydrophobicity, (iii) electric dipole moment. bacterial here biased move relatively freely interior, whereas human counterparts more easily stick. Even so, respond predictably mutation, allowing us tune intermix protein's behavior at will. findings how evolution can swiftly optimize diffuse background encounter complexes just single-point mutations, provide rational framework for adjusting cytoplasmic individual proteins, e.g., rescuing poor NMR signals optimizing therapeutics.