Membrane proteins enter the fold

Membrane proteins have historically been recalcitrant to biophysical folding studies. However, recent adaptations of methods from the soluble protein folding field have found success in their applications to transmembrane proteins composed of both alpha-helical and beta-barrel conformations. Avoiding aggregation is critical for the success of these experiments. Altogether these studies are leading to discoveries of folding trajectories, foundational stabilizing forces and better-defined endpoints that enable more accurate interpretation of thermodynamic data. Increased information on membrane protein folding in the cell shows that the emerging biophysical principles are largely recapitulated even in the complex biological environment.

Automated summary

Membrane protein folding studies have historically been challenging, but recent adaptations of methods have led to success in studying transmembrane proteins. Avoiding aggregation is crucial for the success of these experiments, and they have provided insights into folding trajectories, stabilizing forces, and more defined endpoints.Increased understanding of membrane protein folding in the cell has shown that emerging biophysical principles are largely recapitulated even in complex biological environments.