Guanidine hydrochloride-induced folding of proteins.

doi:10.1006/JMBI.1993.1272

Paper

Guanidine hydrochloride-induced folding of proteins.

Published May 20, 1993 · Y. Hagihara, Saburo Aimoto, Anthony L. Fink

Journal of molecular biology

Q1 SJR score

108

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0

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Abstract

Guanidine hydrochloride (Gdn-HCl) is the most commonly used denaturant for proteins. Contrary to expectation, we found that Gdn-HCl at low concentrations refolds acid-unfolded apomyoglobin and cytochrome c, stabilizing the molten globule state, i.e. a compact denatured state with a significant amount of secondary structure, but substantially disordered tertiary structure. A further increase in Gdn-HCl concentration, above 1 M, caused co-operative unfolding of the molten globule state. Similar sequential folding and unfolding transitions were also observed at neutral pH with a synthetic amphiphilic peptide consisting of Lys and Leu residues, indicating the generality of the phenomenon. Although the Gdn-HCl-induced refolding and unfolding transitions were puzzling at first glance, we show that they are readily interpreted in terms of the differential action of Gdn-HCl. We also show that the comparison of the unfolding curves for the molten globule and native states provides a measure of the buried surface area upon formation of the molten globule state.

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Study Snapshot

Guanidine hydrochloride can refold acid-unfolded proteins, stabilizing the molten globule state, and cause co-operative unfolding at higher concentrations, indicating differential action of the denaturant.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

Guanidine hydrochloride-induced folding of proteins.

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