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Updated: Aug 14, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Microrheological detection of protein unfolding
Raymond S Tu1, Victor Breedveld
1School of Chemical & Biomolecular Engineering, Georgia Institute of Technology, 311 Ferst Drive, N.W., Atlanta, Georgia 30332, USA.
Abstract:
We apply passive probes to protein solutions and evaluate the viscous response to folding and unfolding, allowing us to accurately quantify both the thermodynamics of protein folding and the structural dimensions of the protein molecules with subnanometer resolution. Hard-sphere approximations predict a measurable change in relative viscosity as the hydrodynamic volume fraction of protein molecules increases during unfolding. Microrheology measures these changes to unambiguously evaluate the ensemble average characteristics of the unfolded state in a denaturant, urea, while minimizing the shear-induced unfolding and alignment associated with conventional rheometry.
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