The role of the structural motif in a protein folding reaction: Comparison of the folding mechanisms of alpha/beta sheet proteins

To elucidate the common features of the folding of the ;The urea-induced equilibrium unfolding transitions for the ternary, binary and apo forms of p21;Stopped-flow fluorescence studies of the folding of hDHFR reveal two slow folding reactions. Several lines of evidence of cofactor binding and chaperone protein GroEL binding studies further confirm that the folding of hDHFR follows two parallel channels in which a pair of intermediates and two native conformers are involved. The difference between the two folding models involves the binding affinity of the early intermediate of hDHFR for the substrates.;The similarity of the folding kinetics between the ras protein and the DHFRs suggests that the folding reaction are possibly motif-specific rather than sequence-specific for the...