HYDROGEN-EXCHANGE RATES AND PROTEIN-FOLDING

Transient folding intermediates have been monitored in 11 proteins by pulsed hydrogen exchange methods. Standard hydrogen isotope exchange k inetics have also been measured for several molten globules. Taken tog ether with folding kinetics detected by optical techniques, and with h ydrogen exchange kinetics in native proteins, the results permit concl usions about time constants, structure and stability of folding interm ediates, and about parallel versus serial folding pathways.