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Nathalie Sonveaux
Researcher at Université libre de Bruxelles
Publications - 6
Citations - 487
Nathalie Sonveaux is an academic researcher from Université libre de Bruxelles. The author has contributed to research in topics: Protein structure & Protein tertiary structure. The author has an hindex of 5, co-authored 6 publications receiving 479 citations. Previous affiliations of Nathalie Sonveaux include BC Cancer Research Centre.
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Journal ArticleDOI
Structural Characterization of the Hydrophobin SC3, as a Monomer and after Self-Assembly at Hydrophobic/Hydrophilic Interfaces
Marcel L. de Vocht,Karin Scholtmeijer,Eric W. van der Vegte,Onno M. H. de Vries,Nathalie Sonveaux,Han A. B. Wösten,Jean Marie Ruysschaert,Georges Hadziioannou,Joseph G. H. Wessels,George T. Robillard +9 more
TL;DR: It is determined that the hydrophobin SC3 from Schizophyllum commune contains 16-22 O-linked mannose residues, probably attached to the N-terminal part of the peptide chain, and that Alpha-helix is induced specifically upon assembly of the protein on a hydrophobic solid surface.
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Secondary and Tertiary Structure Changes of Reconstituted P-glycoprotein A FOURIER TRANSFORM ATTENUATED TOTAL REFLECTION INFRARED SPECTROSCOPY ANALYSIS
TL;DR: Fluorescence quenching experiments confirmed that MgATP-induced changes are to be found in the tertiary structure of the enzyme.
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Ligand-mediated Tertiary Structure Changes of Reconstituted P-glycoprotein A TRYPTOPHAN FLUORESCENCE QUENCHING ANALYSIS
TL;DR: Different conformational states were adopted by P-glycoprotein upon the addition of the anthracycline derivatives in the absence and presence of MgATP or MgatPγS, and these conformational changes are shown to be related to the nature of the antitumor agents and more precisely to their capacity to accumulate in resistant cells.
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The topology of the S protein in the yeast-derived hepatitis B surface antigen particles.
Nathalie Sonveaux,Katja Conrath,Carine Capiau,Robert Brasseur,Erik Goormaghtigh,Jean Marie Ruysschaert +5 more
TL;DR: The FTIR spectra of the digested hepatitis B particles revealed that the peptides associated with the particles are rich in alpha-helix structure, and the kinetic of 2H/H exchange provided evidence that a large fraction of the native S protein is poorly accessible to the aqueous medium.
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Characterization of the HBsAg particle lipid membrane.
TL;DR: The data strongly suggest that the HBsAg particle membrane is organized as a discontinuous rigid bilayer of lipids interacting with protein aggregates.