Modulating uranium binding affinity in engineered calmodulin EF-hand peptides: effect of phosphorylation

To improve our understanding of uranium toxicity, the determinants of uranyl affinity in proteins must be better characterized. In this work, we analyzed the contribution of a phosphoryl group on uranium binding affinity in a protein binding site, using the site 1 EF-hand motif of calmodulin. The re...

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Bibliographic Details
Published in:	PloS one Vol. 7; no. 8; p. e41922
Main Authors:	Pardoux, Romain, Sauge-Merle, Sandrine, Lemaire, David, Delangle, Pascale, Guilloreau, Luc, Adriano, Jean-Marc, Berthomieu, Catherine
Format:	Journal Article
Language:	English
Published:	United States Public Library of Science 03-08-2012 Public Library of Science (PLoS)
Subjects:	Affinity Amino acids Analysis Arabidopsis - chemistry Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis thaliana Binding sites Biochemistry Biochemistry, Molecular Biology Biology Calcium Calcium-binding protein Calmodulin Calmodulin - chemistry Calmodulin - genetics Calmodulin - metabolism Casein kinase II Casein Kinase II - chemistry Casein Kinase II - genetics Casein Kinase II - metabolism Catalysis Chemistry Chromatography Dissociation EF-hand Environmental Engineering Environmental Sciences Fluorescence Homogeneity Hydrogen ions Hydrogen-Ion Concentration Ion-exchange chromatography Kinases Life Sciences Ligands Paramecium Peptides pH effects Phosphorylation Physical chemistry Physiological aspects Protein Binding Protein Engineering Protein kinase C Protein kinases Protein Structure, Tertiary Proteins Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Spectrometry Threonine Toxicity Tyrosine Uranium Uranium - chemistry Uranium - metabolism Uranium - toxicity Uranium dioxide Vibration France peptides uranyl binding site phosphoryl group
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