"Partly Folded" State, a New Equilibrium State of Protein Molecules: Four-state Guanidinium Chloride-induced Unfolding of .Beta.-lactamase at Low Temperature
Document Type
Article
Publication Date
1994
Digital Object Identifier (DOI)
https://doi.org/10.1021/bi00176a006
Abstract
The Guanidinium chloride (GdmCl)-induced unfolding of β-lactamase has been investigated using a combination of size-exclusion chromatography (SEC-FPLC) and traditional optical methods. It has been shown that at low temperatures, this protein unfolds through two equilibrium intermediates. The first of these intermediates is the molten globule state, while the other (which we have called a "partly folded" state) is less compact than the molten globule but much more compact than the unfolded state. It also preserves a substantial part of the secondary structure of the native or molten globule state.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biochemistry, v. 33, issue 10, p. 2782-2791
Scholar Commons Citation
Uversky, Vladimir N. and Ptitsyn, Oleg B., ""Partly Folded" State, a New Equilibrium State of Protein Molecules: Four-state Guanidinium Chloride-induced Unfolding of .Beta.-lactamase at Low Temperature" (1994). Molecular Medicine Faculty Publications. 629.
https://digitalcommons.usf.edu/mme_facpub/629
