Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Effects of cavity-forming mutations on the internal dynamics of azurin.

Biophysical journal - 1 Feb 2004

Cioni Patrizia, de Waal Ellen, Canters Gerard W, Strambini Giovanni B

Abstract excerpt

The effects of two single-point cavity-forming mutations, F110S and I7S, on the internal dynamics of azurin from Pseudomonas aeruginosa were probed by the phosphorescence emission of Trp-48, deeply buried in the compact hydrophobic core of the macromolecule. Changes in flexibility of the protein matrix around the chromophore were monitored by the intrinsic phosphorescence lifetime (tau(0)) whereas more general...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acrylamide
Share to Amino Acid Substitution
Share to Porosity

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

Share to Protein Conformation

Share to Protein Folding

Share to Structure-Activity Relationship

Share to Temperature

Share to Tryptophan

Source

Open in PubMed Open full text

Identifiers

PMID: 14747349
DOI: 10.1016/s0006-3495(04)74189-2
PMCID: PMC1303907

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of cavity-forming mutations on the internal dynamics of azurin.PMID 14747349Read ↗

Time-resolved fluorescence study of azurin variants: conformational heterogeneity and tryptophan mobility.Semantic proximity Read ↗

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

X-ray crystal structure of the two site-specific mutants Ile7Ser and Phe110Ser of azurin from Pseudomonas aeruginosa.Semantic proximity Read ↗

If space is provided, bulky modification on the rim of azurin's beta-barrel results in folded protein.Semantic proximity Read ↗

The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core.Semantic proximity Read ↗

Apo-azurin folds via an intermediate that resembles the molten-globule.Semantic proximity Read ↗

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa.Semantic proximity Read ↗

The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin.Semantic proximity Read ↗

Structural heterogeneity of blue copper proteins: an EPR study of amicyanin and of wild-type and Cys3Ala/Cys26Ala mutant azurin.Semantic proximity Read ↗

Phi-value analysis of apo-azurin folding: comparison between experiment and theory.Semantic proximity Read ↗

Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly.Semantic proximity Read ↗

Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.