Abstract
A study of protein assembly in solution with single-particle imaging and reconstruction techniques using cryoelectron microscopy is reported. The human glutamine synthetase enzyme, important in brain metabolism, and previously assumed to be assembled into a homogeneous quaternary structure, is found to be heterogeneous, with three oligomeric states that co-exist at room temperature. This result corrects an old structural and kinetic model determined by ensemble averaging techniques that assumed a homogeneous system. Unexpectedly fast protein dissociation kinetics results from a stabilized transition state.
- Received 14 December 2000
DOI:https://doi.org/10.1103/PhysRevE.64.041911
©2001 American Physical Society