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Updated: Jul 12, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions
Xuanjun Ai1, Zheng Zhou, Yawen Bai
1Department of Biochemistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.
Abstract:
The effects of macromolecular crowding on protein stability and folding kinetics have been studied using the recently developed 15N spin relaxation dispersion technique. By applying this method to a redesigned apocytochrome b562, the kinetics and thermodynamics of the protein folding processes in both the presence and the absence of crowding agents have been characterized. The result indicates that, even under the mild crowded environments (in the presence of 85 mg/mL of PEG 20K), the folding rate of the protein can speed up significantly while the unfolded rate remains unchanged within experimental error.
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