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
Scholar Commons Citation
Uversky, Vladimir N.; Segel, Daniel J.; Doniach, Sebastian; and Fink, Anthony L., "Association-induced Folding of Globular Proteins" (1998). Molecular Medicine Faculty Publications. 645.
https://digitalcommons.usf.edu/mme_facpub/645
