First Paragraph of Review of Paper Comparing Protein folding in vitro and in vivo

This review, authored by Dr. Hingorani and Dr. Gierasch, aims to link fundamental research regarding in vitro and in vivo protein folding in an evolutionary context. Since RNaseA was first denatured and re-folded sixty years ago, studies regarding in vitro protein folding have advanced our understanding of the process of protein folding specifically of small fast-folding domains, which could shed light on their in vivo folding properties and function in large proteins and the proteome as a whole. Strides have also been made in understanding the purpose and nature of unfolded protein states in vitro. Despite tremendous advances in the understanding of protein folding in vitro, there are still so many factors manufactured by the cells diverse and adaptive environment that cannot be simulated in highly diluted conditions. Factors such as chaperone and degradation enzyme aided folding, co-translational folding, crowding/ protein-protein interactions are all vital factors that affect how a protein folds and can only exist in vivo.