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Proc Natl Acad Sci U S A. 1998 May 12;95(10):5480-3.

Association-induced folding of globular proteins.

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  • 1Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064, USA. uversky@sun.ipr.serpukhov.su


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 conditions the association of partially folded intermediates can induce additional structure leading to soluble aggregates with many native-like properties. 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 concentrations. In addition, more globularity, as determined from Kratky plots of small-angle x-ray scattering data, was also noted in the associated states.

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