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Article

Perturbed pKA-values in the denatured states of proteins.

Journal of molecular biology - 15 Dec 1995

Tan Y J, Oliveberg M, Davis B, Fersht A R

Abstract excerpt

We show in this study that the ionisation equilibria of denatured proteins in pure water are inconsistent with the "fully-unfolded" conformation being an extended coil where the residues are isolated from one another by the intervening solvent. The effects of acid and salt on the stability of the barley chymotrypsin inhibitor 2 (CI2) were investigated and the pKA-values of all carboxylate residues in the native...

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Identifiers

PMID: 7500365
DOI: 10.1006/jmbi.1995.0670

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Perturbed pKA-values in the denatured states of proteins.PMID 7500365Read ↗

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pK(a) values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability.Semantic proximity Read ↗

Highly perturbed pKa values in the unfolded state of hen egg white lysozyme.Semantic proximity Read ↗

Conformation and stability of barley chymotrypsin inhibitor-2 (CI-2) mutants containing multiple lysine substitutions.Semantic proximity Read ↗

Uncovering specific electrostatic interactions in the denatured states of proteins.Semantic proximity Read ↗

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Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.Semantic proximity Read ↗

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