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Article

Effect of Lys-->Arg mutation on the thermal stability of Cu,Zn superoxide dismutase: influence on the monomer-dimer equilibrium.

Protein engineering - 1 Apr 1996

Folcarelli S, Battistoni A, Carrì M T, Polticelli F, Falconi M, Nicolini L, Stella L, Rosato N, Rotilio G, Desideri A

Abstract excerpt

The thermal stability of two single (K3R, K67R) and one double (K3R-K67R) mutants of Xenopus laevis B Cu, Zn superoxide dismutase has been studied to test Lys --> Arg substitution as an 'electrostatically conservative' strategy to increase protein stability. The K3R mutant displays an increased thermostability with respect to the wild-type enzyme, whilst a decreased stability was observed in the case of the K67R...

Read the complete abstract on PubMed

Topics

Animals
Arginine
Computer Simulation
Enzyme Stability
Lysine
Models, Molecular

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Mutation

Superoxide Dismutase

Xenopus laevis

Source

Identifiers

PMID: 8738207
DOI: 10.1093/protein/9.4.323

Provenance

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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