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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Jan;87(2):573–577. doi: 10.1073/pnas.87.2.573

Acid-induced folding of proteins.

Y Goto 1, L J Calciano 1, A L Fink 1
PMCID: PMC53307  PMID: 2153957

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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