Desolvation Energy: A Rationale for Changes in Binding Affinity as Measured by ITC

Abstract

The cell is highly crowded with biomacromolecules, and the excluded volume influences processes such as diffusion, folding, conformation, and aggregation or association of proteins and polynucleic acids. In Escherichia coli, the values reported for the total macromolecular content range from 200 to 400 mg/mL. Knowledge of the macromolecular crowding is needed to understand behavior and especially interactions of biomolecules in vivo, be it for drug development, fundamental knowledge, or to support computational efforts to model the living cell. Direct spatiotemporal readout of the crowding would be a powerful asset to unravel the structure of the cytoplasm and the impact of excluded volume on protein function in living cells. Here, we introduce a Förster resonance energy transfer (FRET) sensor for quantification of the macromolecular crowding and apply the sensor in living cells.

Applications of isothermal titration calorimetry - the research and technical developments from 2011 to 2015

“…This number of papers is impractical to cite in full so the author has selected approximately 200 that he feels best represents the field and apologizes for any resulting omissions. These references have been classified into the following broad categories: references cited in the introduction, review and perspective articles, methods papers, protein : protein interactions, protein interactions with other ligands, lipids, micelles and membranes, polysaccharides, nucleic acids, synthetic chemicals, polymers and nanoparticles,…”