Binary and ternary aggregation within tethered protein constructs

Yuan Yang Wei, Martin Gruebele

Research output: Contribution to journalArticlepeer-review

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, ΔΔG(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 ΔΔG(2) = -3.1 kT between dimer and trimer.

Original languageEnglish (US)
Pages (from-to)2930-2937
Number of pages8
JournalBiophysical journal
Volume90
Issue number8
DOIs
StatePublished - Apr 2006

ASJC Scopus subject areas

  • Biophysics

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