Coarse-grained simulation of PEGylated and tethered protein devices at all experimentally accessible surface residues on β-lactamase for stability analysis and comparison

PEGylated and surface-tethered proteins are used in a variety of biotechnological applications, but traditional methods offer little control over the placement functionalization sites on protein. Fortunately, recent experimental functionalize protein at any location amino acid sequence, so question becomes one selecting site that will result best function. This work shows how molecular simulation can be to screen potential attachment for surface tethering or PEGylation. Previous has shown promise this regard model protein, these studies limited screening only few surface-accessible considered PEGylation separately rather than their combined effects. is done overcome limitations by all industrial therapeutic importance (TEM-1) evaluate effects simultaneously an effort create more accurate screen. The results show effectiveness appears function super-secondary tertiary structures primary structure, as often currently assumed. Moreover, middle secondary structure elements, not those loops regions, good options functionalization—a fact appreciated current practice. Taken whole, rigorous identify candidate acids facilitate rational design devices.