Thermodynamic, structural and functional properties of membrane protein inclusion bodies are analogous to purified counterparts: case study from bacteria and humans

摘要: Structural and biophysical characterization of transmembrane proteins that require sufficiently pure protein in high amounts are usually generated large-scale preparations as inclusion bodies (IBs). However, IB subsequent purification, is oftentimes laborious, painstaking, time-consuming, expensive demands protein-dependent customization. We demonstrate purification dispensable if IBs pure; the latter can be directly used functional experiments. Using an assortment membrane from bacteria humans, we validate their purified counterparts exhibit analogous structure, stability, thermodynamic parameters well channel conductance activity. Direct use crude by circumventing could find immediate application speedy generation high-throughput mutant libraries β-barrels, possibly helical proteins.