Protein-complex stability in cells and in vitro under crowded conditions

Biology is beginning to appreciate the effects of the crowded and complex intracellular environment on the equilibrium thermodynamics and kinetics of protein folding. The next logical step involves the interactions between proteins. We review quantitative, wet-experiment based efforts aimed at understanding how and why high concentrations of small molecules, synthetic polymers, biologically relevant cosolutes and the interior of living cells affect the energetics of protein-protein interactions. We then address popular theories used to explain the effects and suggest expeditious paths for a more methodical integration of experiment and simulation.

Automated summary

Biology is starting to understand the impact of crowded and complex intracellular environments on the thermodynamics and kinetics of protein folding, with a focus on protein-protein interactions. The study reviews experimental efforts to quantify how various molecules and cell interiors affect these interactions, and proposes integrating experiments and simulations for better understanding.