Binary and ternary aggregation within tethered protein constructs
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Updated: Aug 10, 2026

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment
Published on: April 20, 2018
Wei Yuan Yang1, Martin Gruebele
1Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Champaign, 61801, USA.
Abstract:
The free energy per monomer of a protein aggregate varies with the number of participating monomers n. The change of this free energy with aggregate size, DeltaDeltaG(n), is difficult to determine by sedimentation or concentration studies. We introduce a kinetic approach to quantitate the free energy of aggregates in the presence of tethers. By linking the protein U1A into dimers and trimers, a high effective concentration of the monomers is achieved, together with exact size control of the aggregates. We found that the free energy of the aggregate relative to the native monomer reached a maximum for n = 2, and decreased by DeltaDeltaG(2) = -3.1 kT between dimer and trimer.
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