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Article

Probing the influence on folding behavior of structurally conserved core residues in P. aeruginosa apo-azurin.

Protein science : a publication of the Protein Society - 1 Oct 2004

Engman K Cecilia, Sandberg Anders, Leckner Johan, Karlsson B Göran

Abstract excerpt

The effects on folding kinetics and equilibrium stability of core mutations in the apo-mutant C112S of azurin from Pseudomonas aeruginosa were studied. A number of conserved residues within the cupredoxin family were recognized by sequential alignment as constituting a common hydrophobic core: I7, F15, L33, W48, F110, L50, V95, and V31. Of these, I7, V31, L33, and L50 were mutated for the purpose of obtaining...

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Identifiers

PMID: 15340166
DOI: 10.1110/ps.04849004
PMCID: PMC2286540

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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