Kinetic experiments using a new generation of techniques with dramatically improved time resolution have contributed significantly to our understanding of mechanisms in protein folding. Optical triggering with nanosecond laser pulses and improvement in the time resolution of mixing experiments has made it possible to study the fastest-folding proteins as well as fundamental processes in folding for the first time. These include formation of alpha-helices, beta-sheets, and contacts between residues distant in sequence, as well as overall collapse of the polypeptide chain. Simple statistical mechanical models have been developed which are extremely useful in interpreting the experimental results. One of the surprises is that a model developed for explaining the fast kinetics of secondary structure formation in isolated peptides is also successful in calculating folding rates of small proteins from their native structure.
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