Single-particle study of protein assembly

Ching-Hwa Kiang
Phys. Rev. E 64, 041911 – Published 24 September 2001
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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

Authors & Affiliations

Ching-Hwa Kiang

  • Physics Department, University of California, Los Angeles, California 90095

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Vol. 64, Iss. 4 — October 2001

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