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. 1990 Jan;87(2):573-7.
doi: 10.1073/pnas.87.2.573.

Acid-induced folding of proteins

Y Goto  1 , L J Calciano, A L Fink
Affiliations

Acid-induced folding of proteins

Y Goto et al. Proc Natl Acad Sci U S A. 1990 Jan.

Abstract

The addition of HCl, at low ionic strength, to the native state of apomyoglobin, beta-lactamase, and cytochrome c caused these proteins to adopt an essentially fully unfolded conformation in the vicinity of pH 2. However, contrary to expectation, the addition of further acid resulted in refolding to a compact conformation with the properties of a molten globule. The major factor responsible for the refolding is believed to be the binding of the anion, which minimizes the intramolecular charge repulsion that initially brought about the unfolding.

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