ArticleBiophysical journal2008
Cavity-creating mutations in Pseudomonas aeruginosa azurin: effects on protein dynamics and stability.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Redesign of γ-glutamyl transpeptidase from Bacillus subtilis for high-level production of L-theanine by cavity topology engineering.Applied microbiology and biotechnology · 2023Article
- Inside Out Computational Redesign of Cavities for Improving Thermostability and Catalytic Activity ofApplied and environmental microbiology · 2023Article
- Photoinduced Electron Transfer from the Tryptophan Triplet State in Zn-Azurin.ACS physical chemistry Au · 2023Article
- Tuning Structure and Dynamics of Blue Copper Azurin Junctions via Single Amino-Acid Mutations.Biomolecules · 2019Article
- Beta-barrel scaffold of fluorescent proteins: folding, stability and role in chromophore formation.International review of cell and molecular biology · 2013Review
- Phenotypic effects of Ehlers-Danlos syndrome-associated mutation on the FnIII domain of tenascin-X.Protein science : a publication of the Protein Society · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Changes in flexibility and structural stability of Pseudomonas aeruginosa azurin in response to cavity-creating mutations were probed by the phosphorescence emission of Trp-48, which was deeply buried in the compact hydrophobic core of the macromolecule, and by measurements of guanidinum hydrochloride unfolding, respectively. Replacement of the bulky side chains Phe-110, Phe-29, and Tyr-108 with the smaller Ala introduced cavities at different distances from the hydrophobic core. The phosphorescence lifetime (tau(0)) of Trp-48, buried inside the protein core, and the acrylamide quenching rate constant (k(q)) were used to monitor local and global flexibility changes induced by the introduction of the cavity. The results of this work demonstrate the following: 1), the effect on core flexibility of the insertion of cavities is not correlated readily to the distance of the cavity from the core; 2), the protein global flexibility results are related to the cavity distance from the packed core of the macromolecule; and 3), the increase in protein flexibility does not correspond necessarily to a comparable destabilizing effect of some mutations.
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Registered trials
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