ASSOCIATION-INDUCED FOLDING OF GLOBULAR-PROTEINS

It has generally been assumed that the aggregation of partially folded intermediates during protein refolding results in the termination of further protein folding, We show here, however, that under some condit ions the association of partially folded intermediates can induce addi tional structure leading to soluble aggregates with many native-like p roperties, The amount of secondary structure in a monomeric, partially folded intermediate of staphylococcal nuclease was found to double on formation of soluble aggregates at high protein or salt concentration s. In addition, more globularity, as determined from Kratky plots of s mall-angle x-ray scattering data, was also noted in the associated sta tes.