Protein Fold

For in-vitro experiments, small fast-folding domains are most preferred as they are amenable to a great extent to observe the detailed physio-chemical behavior of R-groups and other primary, secondary, or tertiary interactions. However, small single domain proteins are very rare, and recent studies have suggested that the folding of domains in multi-domain proteins may not even be an independent process (if we look at the folding of domains as component of a larger protein). Thus, recent studies have tried to focus on in-vitro protein folding of larger proteins, and the results confirm the hypothesis that new complexities in folding landscape will emerge when multiple domains are interacting.