Enzymatic activity outside the folded states of proteins

While the role of protein dynamics in enzyme catalysis has been widely recognised, evidence is now accumulating against the traditional view that enzymes require well defined folded structures for their enzymatic activity. Enzymatically active protein molecules have been found to populate a number of conformations, ranging from partially structured states with molten globule features to fully unfolded ensembles. This may have important implications for our understanding of catalysis, for the study of the possible roles played by natively unfolded proteins and possibly for the search of novel enzymes of biotechnological and industrial interest.