Title

Association-induced Folding of Globular Proteins

Document Type

Article

Publication Date

1998

Digital Object Identifier (DOI)

https://doi.org/10.1073/pnas.95.10.5480

Abstract

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.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Biochemistry, v. 95, issue 10, p. 5480-5483

Share

COinS