How do denatured proteins refold in the test tube?
It has been evident for many years that the sequence of a protein defines its three-dimensional fold. The question of how an unstructured (random coil) polypeptide can rapidly and efficiently find its appropriate fold from the countless alternatives is, however, a problem that has perplexed the scientific community for many years. Considerable progress in understanding this remarkable process has been made recently through a combination of theoretical and experimental advances.A particularly important theoretical strategy has been to simulate refolding by using ‘lattice models’ for proteins in which residues are represented as points on a three-dimensional lattice that interact with one another according to defined potential functions. The idea is to devise models simple enough for extensive calculations to be carried out to simulate refolding, yet sufficiently complex to encapsulate key features of real proteins. Martin Karplus (Cambridge, MA) described the results of simulations usin
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