Abstract
The use of protein engineering in combination with fast kinetics to obtain information about the transition state and intermediates in the folding reaction of globular proteins is re-examined. This method yields information complementary to the quenched-flow NMR technique, but suffers from many of the same limitations. Combined use of quenched-flow NMR and protein engineering offers a picture of the kinetic folding intermediate that differs in some way from that of an equilibrium molten globule.
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