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Binary and Ternary Aggregation within Tethered Protein Constructs

Authors
Journal
Biophysical Journal
0006-3495
Publisher
Elsevier
Publication Date
Volume
90
Issue
8
Identifiers
DOI: 10.1529/biophysj.105.075846
Keywords
  • Proteins
Disciplines
  • Biology

Abstract

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, ΔΔ G( 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 ΔΔ G(2) = −3.1 kT between dimer and trimer.

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