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Article

pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme.

Biochemistry - 6 Mar 1990

Anderson D E, Becktel W J, Dahlquist F W

Abstract excerpt

The energetics of a salt bridge formed between the side chains of aspartic acid 70 (Asp70) and histidine 31 (His31) of T4 lysozyme have been examined by nuclear magnetic resonance techniques. The pKa values of the residues in the native state are perturbed from their values in the unfolded protein such that His31 has a pKa value of 9.1 in the native state and 6.8 in the unfolded state at 10 degrees C in moderate...

Topics

Aspartic Acid
Histidine
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Models, Molecular
Muramidase
Mutation
Potassium Chloride
Protein Conformation
Protein Denaturation
T-Phages

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Thermodynamics

X-Ray Diffraction

Source

Identifiers

PMID: 2337607
DOI: 10.1021/bi00461a025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2337607-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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