J
Javier Pérez
Researcher at Soleil Synchrotron
Publications - 48
Citations - 2102
Javier Pérez is an academic researcher from Soleil Synchrotron. The author has contributed to research in topics: Protein structure & Transfer RNA. The author has an hindex of 24, co-authored 48 publications receiving 1860 citations. Previous affiliations of Javier Pérez include Centre national de la recherche scientifique & University of Paris-Sud.
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Journal ArticleDOI
NADPH oxidase activator p67phox behaves in solution as a multidomain protein with semi-flexible linkers
Dominique Durand,Corinne Vivès,Corinne Vivès,Dominique Cannella,Dominique Cannella,Javier Pérez,Eva Pebay-Peyroula,Eva Pebay-Peyroula,Patrice Vachette,Patrice Vachette,Franck Fieschi,Franck Fieschi +11 more
TL;DR: The SAXS analysis of p67(phox) reveals that it behaves as a multidomain protein with semi-flexible linkers and suggests that the protein is not as extended as unstructured linkers could allow, thereby implying the existence of intra-molecular interactions within p67 (phox).
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Evolution of the Internal Dynamics of Two Globular Proteins from Dry Powder to Solution
TL;DR: Myoglobin and lysozyme picosecond internal dynamics in solution is compared to that in hydrated powders by quasielastic incoherent neutron scattering to derive information on the amount of local diffusive motions and their characteristic average relaxation time.
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How to Squeeze a Sponge: Casein Micelles under Osmotic Stress, a SAXS Study
Antoine Bouchoux,Antoine Bouchoux,Geneviève Gésan-Guiziou,Geneviève Gésan-Guiziou,Javier Pérez,Bernard Cabane +5 more
TL;DR: By combining the osmotic stress technique with small-angle x-ray scattering measurements, the structural response of the casein micelle to an overall increase in concentration is followed, indicating that this compression is nonaffine, i.e., some parts of the micelle collapse, whereas other parts resist deformation.
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Heat-induced unfolding of neocarzinostatin, a small all-beta protein investigated by small-angle X-ray scattering.
TL;DR: The failure of the simple thermodynamic model suggests that there is more than the single intermediate structure required by singular value decomposition analysis, and the classical model of three thermodynamically well-defined states is used to account for the data.
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Aggregation of the salivary proline-rich protein IB5 in the presence of the tannin EgCG.
Francis Canon,Franck Paté,Véronique Cheynier,Pascale Sarni-Manchado,Alexandre Giuliani,Javier Pérez,Dominique Durand,Joaquim Li,Bernard Cabane +8 more
TL;DR: In the mouth, proline-rich proteins (PRP), which are major components of stimulated saliva, interact with tannins contained in food, and in vitro interactions of the tannin epigallocatechin gallate (EgCG) are reported.