Assessing extremophilic proteome refoldability with mass spectrometry

Abstract

Anfinsen's thermodynamic hypothesis postulates that protein structure is encoded in primary sequence, allowing macromolecules to reliably navigate to their native fold by minimizing their Gibb's free energy. This theory implies that protein refolding should spontaneously occur after denaturation. However, exceptions exist; some proteins form aggregates and misfold following denaturation, suggesting that kinetics also plays a significant role in protein folding and assembly. Proteins in extremophilic species can maintain their structures and functions in extreme temperatures.