about
Expression, purification, crystallization and preliminary crystallographic analysis of a deblocking aminopeptidase from Pyrococcus horikoshii.Assessing protein disorder and induced folding.The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.Understanding the structural ensembles of a highly extended disordered protein.Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering.UV and X-ray structural studies of a 101-residue long Tat protein from a HIV-1 primary isolate and of its mutated, detoxified, vaccine candidate.The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner.Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes.The C-terminal domain of the measles virus nucleoprotein is intrinsically disordered and folds upon binding to the C-terminal moiety of the phosphoprotein.Synergy, structure and conformational flexibility of hybrid cellulosomes displaying various inter-cohesins linkers.Crystal structure at 1.45-A resolution of the major allergen endo-beta-1,3-glucanase of banana as a molecular basis for the latex-fruit syndrome.
P50
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P50
name
Véronique Receveur-Bréchot
@ast
Véronique Receveur-Bréchot
@en
Véronique Receveur-Bréchot
@nl
type
label
Véronique Receveur-Bréchot
@ast
Véronique Receveur-Bréchot
@en
Véronique Receveur-Bréchot
@nl
prefLabel
Véronique Receveur-Bréchot
@ast
Véronique Receveur-Bréchot
@en
Véronique Receveur-Bréchot
@nl