Related Experiment Video
Updated: Jul 31, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
A thermodynamic study of the 434-repressor N-terminal domain and of its covalently linked dimers
J Ruiz-Sanz1, A Simoncsits, I Törö
1Department of Physical Chemistry, Institute of Biotechnology, Faculty of Sciences, University of Granada, Spain.
Abstract:
The isolated N-terminal 1-69 domain of the 434-phage repressor, R69, and its covalently linked (head-to-tail and tail-to-tail) dimers have been studied by differential scanning microcalorimetry (DSC) and CD. At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. At neutral pH and moderate ionic strength, the domains of the dimers behave as two independent units with unfolding parameters similar to those of the isolated domain, which means that linking two R69 domains, either by a long peptide linker or by a designed C-terminal disulfide bridge, does not induce any cooperation between them.
More Related Videos
09:15Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Related Concept Videos
Cooperative Binding of Transcription Regulators
Co-activators and Co-repressors
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Cooperative Binding of Transcription Regulators
Co-activators and Co-repressors
Repressible Operon: trp Operon