PROTEIN FOLD RECOGNITION

An important, yet seemingly unattainable, goal in structural molecular biology is to be able to predict the native three-dimensional structu re of a protein entirely from its amino acid sequence. Prediction meth ods based on rigorous energy calculations have not yet been successful , and best results have been obtained from homology modelling and stat istical secondary structure prediction. Homology modelling is limited to cases where significant sequence similarity is shared between a pro tein of known structure and the unknown. Secondary structure predictio n methods are not only unreliable, but also do not offer any obvious r oute to the full tertiary structure. Recently, methods have been devel oped whereby entire protein folds are recognized from sequence, even w here little or no sequence similarity is shared between the proteins u nder consideration. In this paper we review the current methods, inclu ding our own, and in particular offer a historical background to their development. In addition, we also discuss the future of these methods and outline the developments under investigation in our laboratory.