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DTSTART;TZID=Europe/Paris:20260608T140000
DTEND;TZID=Europe/Paris:20260608T160000
DTSTAMP:20260529T142409Z
CREATED:20260529T142409Z
LAST-MODIFIED:20260529T142409Z
UID:10000171-1780927200-1780934400@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Antoine CURÉ (IRIG / Symmes)
DESCRIPTION:Vers des copolymères à blocs donneur-accepteur π-conjugués à structure et composition précisément définies : caractérisation avancée et stratégies de synthèse\nRésumé : \nDans un contexte mondial de crise énergétique et de raréfaction des ressources fossiles\, la transition vers les énergies renouvelables constitue un enjeu majeur. Parmi elles\, l’énergie photovoltaïque occupe une place importante. Cependant\, alors que les panneaux solaires au silicium approchent de leurs limites en rendement et en coûts de production\, l’émergence de solutions complémentaires devient nécessaire. Les cellules solaires organiques constituent une alternative intéressante\, avec des rendements atteignant 21 % dans des conditions standard en laboratoire en 2026. Elles présentent également de bonnes performances en lumière diffuse et offrent un potentiel de production à faible coût de dispositifs flexibles et recyclables. Toutefois\, leur stabilité à long terme reste un obstacle à leur industrialisation. La couche active\, composée d’un donneur (polymère) et d’un accepteur (petite molécule)\, subit au cours du temps une séparation de phase qui dégrade les performances. Malgré les progrès réalisés avec les accepteurs polymères\, la viabilité à long terme de ces dispositifs reste à démontrer. ​​​​\n​ Depuis le début des années 2020\, les matériaux monocomposants sont sérieusement envisagés comme une solution à ces problèmes d’instabilité. Contrairement aux mélanges tout-polymères\, ils reposent sur des copolymères à blocs reliant de manière covalente les segments donneurs et accepteurs\, limitant leur mobilité relative et la ségrégation de phase. Si les premières études rapportent des résultats encourageants\, leur structure et leurs propriétés thermiques restent encore mal comprises. La synthèse et l’étude approfondie de ces systèmes constituent l’objectif de cette thèse. ​​​​\nAprès un premier chapitre introductif\, le deuxième chapitre est consacré à l’étude de deux matériaux modèles : le PTQ10\, polymère donneur parmi les plus performants de la littérature\, et le PIDTe\, un polymère accepteur de structure proche de systèmes connus mais dont la synthèse est simplifiée. Ce travail valide leur pertinence comme système modèle et permet de mettre en place les méthodes de caractérisation utilisées dans la suite de la thèse. Le troisième chapitre explore l’analyse structurale des monocomposants par résonance magnétique nucléaire (RMN). L’utilisation de molécules modèles permet d’identifier les signaux caractéristiques des liaisons entre blocs donneurs et accepteurs et d’estimer le nombre moyen de jonctions dans les chaînes de copolymères. Une approche complémentaire par RMN à diffusion ordonnée (DOSY) est également évaluée afin d’estimer la composition des matériaux. Le quatrième chapitre s’intéresse aux propriétés thermiques des monocomposants. Une méthode basée sur la spectroscopie UV-visible est développée pour suivre les évolutions morphologiques à l’échelle nanométrique à l’état solide. Associée à la diffraction des rayons X en incidence rasante (GIWAXS)\, à la microscopie à force atomique (AFM) et à la calorimétrie différentielle à balayage rapide (flash DSC)\, elle permet de comparer la stabilité thermique des monocomposants à celle des mélanges tout-polymères. ​​​​\nEnfin\, le cinquième chapitre vise à synthétiser des monocomposants de structure mieux définie. La modification du monomère du PTQ10 permet d’obtenir un polymère possédant une fonction réactive terminale unique et une structure régiorégulière. Cette régiorégularité améliore l’organisation des chaînes latérales mais semble perturber celle du cœur π-conjugué\, affectant les propriétés optoélectroniques. Différentes stratégies de synthèse de copolymères di- et tri-blocs sont ensuite développées\, ouvrant de nouvelles perspectives. ​​​​\nEn conclusion\, cette thèse contribue à une meilleure compréhension des matériaux monocomposants pour les cellules solaires organiques et propose de nouvelles approches d’analyse et de synthèse pour des dispositifs plus stables et performants. ​​​​ \n_ \nContact : odile.rossignol@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-antoine-cure-irig-symmes/
LOCATION:GreEN-ER – Amphi 2A003\, 21 avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260609T140000
DTEND;TZID=Europe/Paris:20260609T150000
DTSTAMP:20260529T145613Z
CREATED:20260529T143536Z
LAST-MODIFIED:20260529T145613Z
UID:10000173-1781013600-1781017200@sfp-alpes.fr
SUMMARY:Soutenance HDR de Tristan WAGNER (IRIG / IBS)
DESCRIPTION:Characterization of native enzymes to understand how anaerobic microbes impact biogeochemical cycles\nRésumé : \nMicrobes are actors of the biogeochemical cycles\, transforming gases\, minerals\, and biological matter through enzymatic reaction chains. Among them\, anaerobic archaea\, namely methanogens and methanotrophs\, play a key role in converting planetary carbon\, nitrogen\, and sulfur\, impacting the biosphere and providing green sustainable solutions for our modern society. The last fourteen years of my career were devoted to understanding the molecular basis of these microbial transformations\, such as methane production or degradation\, CO2 and carbon monoxide conversion to biofuels\, N2 fixation\, and sulfur cycling. Since these enzymes harbor O2-sensitive complicated metallocofactors\, most of my work relies on native protein purification from the microbes themselves under strict O2 exclusion. After a brief presentation of my career and PhD project\, the presented work summarizes my most renowned breakthrough regarding the elucidation of molecular tricks in carbon\, nitrogen\, and sulfur metabolisms in methane-generating microbes\, including their regulatory networks. Then\, the latest research led by my group is introduced with : (i) how methanogens munch on methylated substrates such as methanol and lignin-degradation products\, (ii) how an industrial bacterium turns waste gases into biofuels\, (iii) the study of a microbial consortia “that burn” methane and ethane without oxygen via a native approach. Finally\, I will present the features of my past group and my future laboratory. ​​ \nL’accès au campus EPN nécessite un avis de rendez-vous. Merci d’adresser votre demande à ibs.seminaires@ibs.fr au moins 48h à l’avance. \nN’oubliez pas de vous munir d’une pièce d’identité.​
URL:https://sfp-alpes.fr/event/tristan-wagner-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260611T113000
DTEND;TZID=Europe/Paris:20260611T123000
DTSTAMP:20260605T140154Z
CREATED:20260605T140154Z
LAST-MODIFIED:20260605T140154Z
UID:10000192-1781177400-1781181000@sfp-alpes.fr
SUMMARY:Kirill NOURSKI (University of Iowa\, USA)
DESCRIPTION:What the insula hears and does : Insights from human intracranial electrophysiology\nRésumé : \nThe human insula is known to be involved in auditory processing\, though its detailed response properties remain elusive. Intracranial recordings in human neurosurgical patients provide a unique opportunity to characterize the functional properties of the human insula with high spatiotemporal resolution. Local field potential recordings reveal that posterior insula (InsP) is characterized by larger broadband gamma (30-150 Hz) responses to monosyllabic words compared to anterior insula (InsA). Both subdivisions of the insula generate evoked responses to novel sounds. Single neurons within InsP and\, to a lesser extent\, InsA\, respond to simple sounds in the absence of a behavioral context. InsP and InsA share similar res9ng state functional connectivity profiles with limbic structures. InsP is more closely linked to activity propagated from early auditory cortex\, while InsA is more tightly coupled with prefrontal\, anterior temporal regions and the amygdala. Clinical case studies identify language and music perception deficiencies associated with insula lesions. Finally\, single unit recordings during emergence from general anesthesia reveal a temporal dissociation between reactivation of limbic structures and the insula\, the laPer marking the transition to connected consciousness and the capacity to act on commands. Together\, these results begin to characterize the insula’s place in the auditory hierarchy\, with implications ranging from sensory processing to conscious awareness of our surroundings. \n_ \nContact : julien.bastin@univ-grenoble-alpes.fr \n  \n 
URL:https://sfp-alpes.fr/event/kirill-nourski-university-of-iowa-usa/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260611T130000
DTEND;TZID=Europe/Paris:20260611T140000
DTSTAMP:20260604T104156Z
CREATED:20260507T093550Z
LAST-MODIFIED:20260604T104156Z
UID:10000147-1781182800-1781186400@sfp-alpes.fr
SUMMARY:Anne LOPES (I2BC - Gif sur Yvette)
DESCRIPTION:Emergence of microproteins and de novo genes from noncoding DNA\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/anne-lopes-i2bc-gif-sur-yvette/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260612T110000
DTEND;TZID=Europe/Paris:20260612T120000
DTSTAMP:20260604T142423Z
CREATED:20260604T142423Z
LAST-MODIFIED:20260604T142423Z
UID:10000187-1781262000-1781265600@sfp-alpes.fr
SUMMARY:Alexandra COLIN (CEA-Irig/LPCV)
DESCRIPTION:Dynamics and Scaling of Competitive Actin Architectures\nRésumé : \n\nCells constantly experience environmental changes requiring a fast adaptation of their different actin structures. However\, the mechanisms governing the size and dynamics of these multiple actin structures remain unknown. Decoupling the various parameters that would provide a complete understanding of these mechanisms is very complicated in a cellular context. This is why we have developed a bottom-up approach to identify the key molecular mechanisms that determine the size and coexistence of multiple competing actin architectures. We used a reconstituted system consisting of purified proteins and substrates to localize actin polymerization in microwells\, enabling us to work with a limited number of components. With this system\, we reconstituted several dynamic actin architectures\, competing for a limited pool of protein\, over a period of multiple hours. This allowed us to gain key insights into physiological functions related to actin turnover. I will show how we used this system to study the limits of scaling in dynamic structures\, as well as the limits of coexistence in actin networks under resource-limited conditions. Finally\, I will show how we can recapitulate these results in a complementary cellular system\, in which we have demonstrated that an increase in spreading area leads to a decrease in overall turnover\, due to a predominance of structures with low turnover.​​​​​\n​\n\n\n\nLes séminaires et soutenances sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire  et de l’adresser\, plus de 48h à l’avance\, à ce contact.\nPensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/alexandra-colin-cea-irig-lpcv/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260615T110000
DTEND;TZID=Europe/Paris:20260615T120000
DTSTAMP:20260529T122925Z
CREATED:20260529T122925Z
LAST-MODIFIED:20260529T122925Z
UID:10000168-1781521200-1781524800@sfp-alpes.fr
SUMMARY:Richard HOLZ (School of Mines\, Golden\, Colorado\, USA)
DESCRIPTION:Targeting Iron-Sulfur Cluster Biosynthesis in Staphylococcus aureus : Mechanistic Insights into the SUF Pathway\n_ \nL’accès au CEA Grenoble nécessite un avis de rendez-vous. Merci d’envoyer la copie de votre pièce d’identité à sandrine.ollagnier@cea.fr\, avant le 08 juin 2026.\nPensez à vous munir de cette pièce d’identité le jour de votre visite. \n  \n 
URL:https://sfp-alpes.fr/event/richard-holz-school-of-mines-golden-colorado-usa/
LOCATION:CEA – Salle de séminaire IRIG (104 – bâtiment C3)\, 17\, avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260618T140000
DTEND;TZID=Europe/Paris:20260618T160000
DTSTAMP:20260529T145529Z
CREATED:20260529T144049Z
LAST-MODIFIED:20260529T145529Z
UID:10000174-1781791200-1781798400@sfp-alpes.fr
SUMMARY:Soutenance HDR de Rebekka WILD (IRIG / IBS)
DESCRIPTION:Molecular insight into the wonderful complex world of protein glycosylation\nRésumé : \nThis research habilitation focuses on the characterization of a class of enzymes – glycosyltransferases – that are involved in the biosynthesis of glycoproteins. It emphasizes the use of cryo-electron microscopy (cryo-EM) to study these enzymes\, for which obtaining mechanistic insights remains a challenging task to this day. The presentation will provide an overview of the different types of glycosylation found in humans\, along with a detailed description of the biosynthetic pathways of N-linked glycans and glycosaminoglycans. Subsequently\, I describe my work over the past ten years\, which is divided into two parts : my postdoctoral studies on a central enzyme complex of the N-linked glycosylation machinery and the work of my research team at the Institut de Biologie Structurale focusing on heparan sulfate and chondroitin sulfate biosynthesis. It closes with an overview on ongoing and future projects.​ \nL’accès au campus EPN nécessite un avis de rendez-vous. Merci d’adresser votre demande à ibs.seminaires@ibs.fr au moins 48h à l’avance. \n\nN’oubliez pas de vous munir d’une pièce d’identité.​
URL:https://sfp-alpes.fr/event/rebekka-wild-irig-ibs/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260618T141500
DTEND;TZID=Europe/Paris:20260618T163000
DTSTAMP:20260529T150945Z
CREATED:20260529T150859Z
LAST-MODIFIED:20260529T150945Z
UID:10000177-1781792100-1781800200@sfp-alpes.fr
SUMMARY:Soutenance de HDR de Andrew GROSS (DCM (équipe BIOCEN))
DESCRIPTION:Nanostructured porous frameworks to control and drive bioelectrocatalysis for sensing and energy generation\n_ \n Contact : Nathalie.Camerino@univ-grenoble-alpes.fr \n 
URL:https://sfp-alpes.fr/event/soutenance-de-hdr-de-andrew-gross-dcm-equipe-biocen/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance HDR
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260619T093000
DTEND;TZID=Europe/Paris:20260619T103000
DTSTAMP:20260529T151254Z
CREATED:20260529T151254Z
LAST-MODIFIED:20260529T151254Z
UID:10000178-1781861400-1781865000@sfp-alpes.fr
SUMMARY:Alain WALCARIUS (Laboratoire de Chimie Physique et Microbiologie pour les Matériaux et l’Environnement (LCPME)\, UMR Université de Lorraine-CNRS 7564\, Equipe Chimie et Electrochimie Analytiques\, Nancy)
DESCRIPTION:Intérêt des membranes de silice à porosité orientée en électrochimie analytique et au delà\n_ \nContact : andrew.gross@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/alain-walcarius-laboratoire-de-chimie-physique-et-microbiologie-pour-les-materiaux-et-lenvironnement-lcpme-umr-universite-de-lorraine-cnrs-7564-equipe-chimie-et-electrochimie-analytiques/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260619T100000
DTEND;TZID=Europe/Paris:20260619T110000
DTSTAMP:20260529T130829Z
CREATED:20260529T130829Z
LAST-MODIFIED:20260529T130829Z
UID:10000169-1781863200-1781866800@sfp-alpes.fr
SUMMARY:Soutenance HDR de Julien PERARD (Irig/LCBM)
DESCRIPTION:From iron to biohydrogen: how bacteria are inspiring the biotechnologies of tomorrow\nRésumé : \nMicroorganisms play a crucial role in biotechnologies\, enabling the transformation of matter into high-value gases and biomass. At a time when the climate emergency demands a rethinking of our energy models\, my work is part of a responsible research approach\, aiming to reconcile scientific excellence\, environmental sustainability\, and economic viability.​\nOver the past twelve years\, I have dedicated my career to understanding the molecular mechanisms of the Fur and SUF systems (Fe-S cluster biogenesis\, bacterial virulence) and to studying nickel insertion into CO dehydrogenase\, using integrated structural approaches (SAXS\, MALLS\, crystallography). Since 2021\, I have refocused my research on energy biotechnologies. After a brief overview of my scientific journey\, I will detail my projects on developing solutions for BioH₂ production and CO₂ valorization\, particularly through the « Bioraffinery » project (combining photofermentation and methanogenesis)\, inspired by my participation in the 2022 EIC Horizon Prize. I have optimized photobioreactors (PBRs)\, improving their light efficiency and achieving up to 5 mol H₂/mol of substrate from PLA waste.​\nToday\, I am working on optimizing microbial strains and culture conditions\, as well as integrating circular processes for the joint production of BioH₂/BioCH₄. In collaboration with Génoscope\, CEA Tech\, and industrial partners\, I have developed advanced biorafineries to convert by-products into biofuels.​\nMy work\, at the interface of biophysics\, enzymology\, and engineering\, is part of a decarbonized bioeconomy approach.​ \n_ \nContact : alain.farchi@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-hdr-de-julien-perard-irig-lcbm/
LOCATION:DCM – Bât Nanobio\, DCM 570 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance HDR
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260622T133000
DTEND;TZID=Europe/Paris:20260622T153000
DTSTAMP:20260604T143528Z
CREATED:20260604T143528Z
LAST-MODIFIED:20260604T143528Z
UID:10000188-1782135000-1782142200@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Khadeeja MUBASHIRA (CEA-Irig/IBS)
DESCRIPTION:Étude de la séparation de phase de la phosphoprotéine du virus de la rage et de sa régulation par LC8\nRésumé : \nRabies virus (RABV) replication occurs in cytoplasmic\, membrane-less compartments known as Negri bodies (NBs)\, formed through liquid-liquid phase separation (LLPS) of viral components. The phosphoprotein (RABV P) is a central\, intrinsically disordered scaf fold of the viral replication machinery. This thesis investigates the structural\, biophysical\, and dynamic properties of RABV P\, with emphasis on its phase separation behavior and interactions with molecular partners. To enable this\, recombinant expression and purification protocols were optimized to produce stable\, high-quality protein samples for reproducible analyses. \nWe first characterized the intrinsic phase behavior of RABV P in vitro. The protein undergoes thermoresponsive LLPS with a lower critical solution temperature (LCST)\, forming reversible condensates within a narrow range of protein and salt concentrations. This process is driven by multivalent interactions within a heterogeneous ensemble of conformations\, where dimers assemble into higher-order oligomers prior to phase separation. The resulting phase diagram reveals a complex\, reentrant system governed by a balance between electrostatic repulsion and attractive dipole-dipole interactions. \nThe role of ionic conditions was further examined. While NaCl induced reentrant phase separation\, LLPS strongly depended on ion identity rather than ionic strength alone. Chloride salts promoted condensate formation\, whereas bromide salts did not\, indicating ion-specific (Hofmeister-type) effects. Systematic trends showed that fluoride enhances phase separation\, while cation effects are weaker. Divalent ions also promoted LLPS\, highlighting valency contributions. Chemical perturbations confirmed that condensates are stabilized by weak interactions: 1\,6-hexanediol partially disrupted droplets\, whereas ATP fully dissolved them. Notably\, RABV P intrinsically phase separates even in water\, modulated by pH\, protein concentration\, and ionic conditions. \nTime-resolved small-angle X-ray scattering (SAXS) revealed the structural evolution underlying LLPS. Following a temperature jump\, RABV P undergoes a hierarchical assembly process\, transitioning from dispersed species to larger structures. Early conformational rearrangements precede the formation of intermediate clusters\, followed by growth into larger assemblies. These structures remain disordered and liquid-like\, supporting a multistep nucleation-and-growth mechanism. \nThe host protein LC8 was investigated as a regulator of RABV P condensation. LC8 binds a conserved motif in RABV P with high affinity\, forming a defined complex and partitioning into condensates. Functionally\, LC8 enhances phase separation by increasing condensate size\, enriching RABV P in the dense phase\, and broadening the phase-separation window. It shifts phase boundaries toward lower concentrations and temperatures while preserving liquid-like properties. These results indicate that LC8 actively promotes condensation by stabilizing interaction-competent conformations and enhancing intermolecular connectivity. \nTo assess whether LC8 can compensate for intrinsic multivalency\, a truncated RABV P lacking the dimerization domain was analyzed. Although LC8 bound this construct\, the interaction was weaker and failed to restore robust phase separation. Only weak condensation was observed under crowding conditions\, demonstrating that LC8 cannot substitute for the native dimerization-driven multivalency.\nOverall\, this work establishes RABV P as a finely tuned multivalent scaffold whose phase behavior arises from the interplay of intrinsic disorder\, ion-specific effects\, and hierarchical assembly. LLPS emerges as a multistep\, non-ideal process rather than a simple binary transition. LC8 acts as a key host regulator that enhances phase separation without altering condensate dynamics\, while intrinsic multivalency remains essential. These findings provide a mechanistic framework for understanding viral condensate formation and highlight potential avenues for antiviral intervention. \n_ \nContact : alain.farchi@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-khadeeja-mubashira-cea-irig-ibs/
LOCATION:Amphi A de Biologie\, Rue de la Piscine\, Saint-Martin-d'Hères\, 38400\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260623T100000
DTEND;TZID=Europe/Paris:20260623T110000
DTSTAMP:20260529T152039Z
CREATED:20260529T151847Z
LAST-MODIFIED:20260529T152039Z
UID:10000179-1782208800-1782212400@sfp-alpes.fr
SUMMARY:Cyril BRESSY (Aix-Marseille Université - Institut des Sciences Moléculaires de Marseille (iSm2))
DESCRIPTION:Compartmentalized MultiCatalysis : Chirality as Probe\, Separation of Enantiomers & Catalytic Active Transport\nRésumé : \nLife solves the problem of different reaction conditions by the compartmentalization of the catalytic systems. This solution opens new opportunities for the chemists using synthetic membranes to isolate the catalytic systems. \nWe were interested to study the diffusion of molecules through a semi-permeable membrane when no gradient of concentration does exist. Chirality was found to be helpful to be used as probe to study such systems (1). A scale of diffusion energy depending on the structure of the solute was established providing fruitful lessons. \nBased on these results\, compartmentalized multicatalytic systems were set up for different goals : \n– A system where two catalysts of opposite configurations are working in each compartment leading to the physical separation of enantiomeric products starting from a racemic substrate. This is describing a case of compartmentalized parallel kinetic resolution (CPKR)(2).\n– A system to promote the active transport of a molecule able to cross a membrane. The active transport means a transfer against the gradient of concentration (3). \nReferences \n1 .  J. Hou\, S. Chevallier-Michaud\, L. Favre\, D. Hérault & C. Bressy\, J. Membrane Sci. 2026\, in revision.\n2  . a) J. Hou\, S. Chevallier-Michaud\, M. Jean\, L. Favre\, D. Hérault & C. Bressy\, J. Am. Chem. Soc. 2023\, 145\, 27236-27241; b) J. Hou\, D. Hérault\, C. Bressy\, “Method for simultaneous preparation of separated enantiomeric products from racemic substrates”\, Extension internationale PCTEP2022085983 (2022) WO2023126186A1.\n3 . Manuscript in preparation \n_ \nContact : adrien.quintard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/cyril-bressy-aix-marseille-universite-institut-des-sciences-moleculaires-de-marseille-ism2/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260625T130000
DTEND;TZID=Europe/Paris:20260625T140000
DTSTAMP:20260612T075402Z
CREATED:20260507T093855Z
LAST-MODIFIED:20260612T075402Z
UID:10000148-1782392400-1782396000@sfp-alpes.fr
SUMMARY:Elodie LAINE (Sorbone Université)
DESCRIPTION:What evolution tells us about the impact of mutations — and how to scale it up\n_ \nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/elodie-laine-sorbone-universite/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260626T110000
DTEND;TZID=Europe/Paris:20260626T120000
DTSTAMP:20260604T145405Z
CREATED:20260604T145405Z
LAST-MODIFIED:20260604T145405Z
UID:10000191-1782471600-1782475200@sfp-alpes.fr
SUMMARY:Christophe MASSELON (CEA-Irig/BGE) et Vincent AGACHE (CEA-Leti/DTIS)
DESCRIPTION:Sensing Mass at the Nanoscale : Suspended Nanochannel Resonators and NEMS-MS for Biology\nRésumé : \n\nDetermining the mass of biological nanoparticles opens new avenues for characterizing biological systems at their own scale. In this joint seminar\, researchers from LETI and IRIG will present two complementary nanoresonator platforms : Suspended Nanochannel Resonators (SNR)\, which operate in solution\, and Nanoelectromechanical Mass Spectrometry (NEMS-MS)\, which operates in the gas phase. Together\, these technologies cover a range of biological particles\, from lipid nanoparticles and extracellular vesicles to viral particles. Beyond the technical principles underlying each platform\, selected applications will illustrate the potential of these approaches for the characterization of biological samples.​​​​​\n​\n\n\n\nLes séminaires et soutenances sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire  et de l’adresser\, plus de 48h à l’avance\, à ce contact.\nPensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/christophe-masselon-cea-irig-bge-et-vincent-agache-cea-leti-dtis/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260626T140000
DTEND;TZID=Europe/Paris:20260626T160000
DTSTAMP:20260529T140307Z
CREATED:20260529T140204Z
LAST-MODIFIED:20260529T140307Z
UID:10000170-1782482400-1782489600@sfp-alpes.fr
SUMMARY:Soutenance de Thèse de Henri GRÖGER (Irig/IBS)
DESCRIPTION:Structural and functional characterisation of the vaccinia virus PLD- fold endonuclease K4\, telomere-binding protein i1 and the DNA polymerase complex E9A20D4\nRésumé : \n\nPoxviruses\, such as the vaccinia virus (VACV) and the monkeypox virus\, are large\, enveloped dsDNA viruses from the orthopoxvirus genus that replicate entirely within the host cytoplasm. The 2022 and 2024 outbreaks of mpox\, caused by clade IIb and Ib\, respectively\, have revealed the lack of efficient antivirals and underlined the urgency of understanding poxvirus biology. The poxvirus genome is flanked by short\, inverted complementary hairpin telomeres that feature mismatched bases and insertions essential for viral replication. ​\n​\nThis thesis presents the structural and functional characterisation of three proteins central to poxvirus DNA metabolism : the E9A20D4 DNA polymerase holoenzyme\, and two telomere-interacting proteins\, the PLD-fold nuclease K4 and I1. The project initially focused on the VACV polymerase holoenzyme\, but was reoriented towards the telomere-interacting proteins following the publication of numerous competing mpox polymerase structures. ​\n​\nHaving established that VACV polymerase activity requires K+ and is inhibited by Na+\, I undertook a structure determination of the E9A20D4 polymerase holoenzyme bound to template DNA\, primer and incoming nucleotide in the presence of K+\, using single-particle cryogenic electron microscopy (cryo-EM). I obtained both the structure of the complex E9exo−A20D4 as well as the structure of E9exo− alone bound to the primer-template DNA. The structures in the presence of K+ appear identical to published structures in the presence of Na+. However\, I identified an ion binding site in the exonuclease domain of E9. The thumb domain is disordered in the DNA-free structure\, partially disordered in DNA-bound E9 and ordered in the holoenzyme-DNA complex. SAXS data indicate conformational flexibility\, with more open conformations of E9A20D4 lacking an E9-D4 interface\, while mass photometry reveals partial dissociation of E9A20D4 at low concentrations\, even in the presence of substrate. ​\n​\nUsing cryo-EM\, I report the first structures of K4 in both apo and DNA-bound states\, revealing that the active site is occluded by an orthopoxvirus-specific C-terminal extension of the PLD fold that is displaced upon DNA binding. Biochemical characterisation demonstrates that K4 functions as a DNA-specific endonuclease with a preference for single-stranded DNA and hairpin loops. ​\n​\nI also report the first cryo-EM structure of I1 bound to DNA. I1 is known to bind to viral telomeres and is essential for virion maturation. Cryo-EM data showed the presence of dimers where the head domains 2 and 3 of I1 interact with the DNA duplex through electrostatic interactions\, while the N-terminal domain predicted to be α-helical remains disordered. In solution\, isolated I1 or I1 bound to DNA forms higher-order assemblies\, predominantly tetramers\, but also octamers. ​\n​\n​ Altogether\, these findings substantially advance the molecular understanding of poxvirus biology\, providing a foundation for future mechanistic studies and the rational development of antiviral strategies against emerging orthopoxvirus infections.\n​​\n\n\nLes séminaires et soutenances sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire  et de l’adresser\, plus de 48h à l’avance\, à ibs.seminaires@ibs.fr. Pensez à vous munir d’une pièce d’identité le jour de votre visite.\n\n  \n  \n  \n  \n  \n 
URL:https://sfp-alpes.fr/event/soutenance-de-these-de-henri-groger-irig-ibs/
LOCATION:Salle des séminaires du CIBB\, EPN Campus - 71 avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260702T113000
DTEND;TZID=Europe/Paris:20260702T123000
DTSTAMP:20260625T134330Z
CREATED:20260625T134330Z
LAST-MODIFIED:20260625T134330Z
UID:10000204-1782991800-1782995400@sfp-alpes.fr
SUMMARY:Soleiman SHOKUR (EPFL\, Lausanne)
DESCRIPTION:Clinical and Functional Benefits of Prosthetics with Multimodal Feedback\nRésumé : \nSomatosensory feedback in prosthetics has advanced considerably\, with invasive and non-invasive approaches now capable of evoking touch and proprioceptive sensations. Yet modalities have largely been studied in isolation\, and thermotactile feedback — the simultaneous combination of touch and temperature — remains unachieved. This is a critical gap : natural touch is inherently multimodal\, and temperature is not merely a tool for object interac4on but a continuous signal through which we monitor our own body. Its absence from prosthetic feedback represents a fundamental impoverishment of the sensory input the brain expects. In this talk\, I will present recent advances in multimodal sensory feedback and discuss its benefits not only for improving prosthetic function and dexterity\, but also for addressing key clinical consequences of amputation — including phantom limb pain and body perception distortion. \n_ \nContact : homaira.nawabi@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/soleiman-shokur-epfl-lausanne/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260703T093000
DTEND;TZID=Europe/Paris:20260703T113000
DTSTAMP:20260625T141107Z
CREATED:20260625T141107Z
LAST-MODIFIED:20260625T141107Z
UID:10000206-1783071000-1783078200@sfp-alpes.fr
SUMMARY:Soutenance de thèse par Léonard OLIVOTTO (CEA-Irig/LCBM)
DESCRIPTION:Conception de catalyseurs hybrides enzyme/nanomatériaux et de solvants sur mesure pour réduire le CO2 par des procédés photochimiques et électrochimiques en présence d’oxygène\nRésumé : \nDans la recherche de nouvelles voies de valorisation du CO2 respectueuses de l’environnement\, l’utilisation d’enzymes représente une approche prometteuse. Parmi elles\, la monoxyde de carbone déshydrogénase (NiFe-CODH) réduit de manière réversible le CO2 en CO avec une performance et une sélectivité remarquable en conditions douces. Pour ces raisons\, plusieurs études ont exploré les [NiFe]-CODH en vue d’applications dans la réduction électrocatalytique et photocatalytique du CO2.\nCependant\, l’extrême sensibilité à l’oxygène de leur site actif constitué d’un centre multimétallique NiFE4S4\, limite leur intégration dans des dispositifs industriels. Par conséquent\, plusieurs stratégies ont été développées pour améliorer la tolérance à l’O2 des systèmes électrocatalytiques et photocatalytiques à base d’enzymes. Parmi celles-ci\, l’utilisation de solvants eutectiques profonds (DES) s’est avérée être une méthode intéressante pour la production photocatalytique d’hydrogène à base d’enzymes. \nDans cette thèse\, plusieurs méthodes de modification de surface pour la conception d’électrodes à base de nanotubes de carbone visant à optimiser l’interface CODH-électrode et\, par conséquent\, à améliorer les performances électrocatalytiques pour la réduction du CO2 ont été développées. Une fois optimisées en milieu aqueux\, les performances des bioélectrodes ont été étudiées dans des DES\, et l’effet protecteur de ce solvant non conventionnel contre l’exposition à l’O2 a été exploré. Les connaissances acquises jusque-là ont finalement été réutilisées pour développer des photosystèmes hybrides semi-conducteur-enzyme (SEHP). Le nitrure de carbone a été modifié par une méthode de greffage au diazonium\, caractérisé et démontré comme coopérant avec la CODH pour réaliser de la photoproduction de CO.\nLe système était également opérationnel dans un DES\, avec des performances catalytiques améliorées\, ce qui laisse entrevoir un avenir prometteur pour le développement de SEHP à base de CODH sensibles à l’O2. \nDans l’ensemble\, ces travaux constituent une nouvelle étape vers l’intégration de biocatalyseurs sensibles à l’O2 dans les technologies pertinentes d’utilisation du CO2. ​​​​ \n_ \nContact : alain.farchi@cea.fr \n 
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-leonard-olivotto-cea-irig-lcbm/
LOCATION:Bâtiment André Rassat / Chimie E – Salle de conférence RDC​\, 470 rue de la Chimie\, Gières\, 38610\, France
CATEGORIES:Soutenance,Soutenance de Thèse
ORGANIZER;CN="IRIG - CEA":MAILTO:odile.rossignol@cea.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260703T110000
DTEND;TZID=Europe/Paris:20260703T120000
DTSTAMP:20260703T084805Z
CREATED:20260626T133757Z
LAST-MODIFIED:20260703T084805Z
UID:10000210-1783076400-1783080000@sfp-alpes.fr
SUMMARY:Catherine ROYER (Rensselaer Polytechnic Institute\, New York)
DESCRIPTION:Pressure-based mapping of protein conformational landscapes\nRésumé : \nProtein function depends upon dynamics\, and while in recent years great progress has been made in predicting protein structure from sequence\, the sequence determinants of functional dynamics have yet to be defined. We have developed an approach using a combination of high-pressure NMR\, SAXS\, fluorescence\, and computation to locally and globally map protein stability and functional dynamics. On a model repeat protein system we find that single amino acid substitutions lead to large changes in local stability and apparent folding cooperativity\, while global stabilities of the variant proteins are similar. In the case of the Arf GTPases\, which undergo massive conformational changes during their nucleotide switch transition\, we demonstrated that the switch mechanism implicates the population of a functional molten globule. Moreover\, we discovered the sequence determinants of back-to-front allosteric control of the switch that differentiates switching probabilities of the Arf family members\, and likely many other small GTPases. \n_ \nCes séminaires\, ainsi que les soutenances et cours sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire et de l’adresser\, plus de 48h à l’avance\, à ce contact. Pensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/catherine-royer-rensselaer-polytechnic-institute-new-york/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260706T110000
DTEND;TZID=Europe/Paris:20260706T120000
DTSTAMP:20260702T131525Z
CREATED:20260702T131457Z
LAST-MODIFIED:20260702T131525Z
UID:10000212-1783335600-1783339200@sfp-alpes.fr
SUMMARY:Guillaume MESTDAGH (INRIA Montbonnot)
DESCRIPTION:Coupling osmosis and mechanics in vertex-based models for plant tissue growth\nRésumé : \nUnderstanding plant growth is fundamental to address global challenges such as food security\, biodiversity\, and soil‑erosion control. The development of plants involves many interconnected physical processes\, occurring at various spatial and temporal scales\, making modeling an indispensable complement to experiments. In particular\, discrete vertex-based models have successfully described the coupling between inter-cell water fluxes and mechanical deformations of cell walls\, in response to a prescribed inner water pressure. \nA two-dimensional vertex-based model represents a group of cells as a tiling of polygons\, with the edges between polygons representing cell walls. Existing vertex-based models postulate a fixed water pressure inside cells as the force driving growth. In reality\, this inner pressure itself is the consequence of osmosis\, a chemical process by which water is attracted into cells with a higher concentration of solute. However\, capturing the interplay between mechanics and solute dynamics in plant tissues into one model remains a challenge that requires novel mathematical frameworks. \nIn this talk\, I will present a new approach to couple solute and water fluxes with mechanics and growth in vertex-based models. The proposed approach is based on a variational formalism where the system physics is described in terms of free energy and dissipation function. After building the model and deriving the evolution equations of the system\, I will show that the resulting formulation can be turned into a numerical method. Finally\, I will illustrate the model properties through a few numerical simulations and discuss its interest for the study of plant growth. \nContact : philippe.marmottant@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/uillaume-mestdagh-inria-montbonnot/
LOCATION:LiPhy – Salle de conférence\, LiPhy 140 avenue de la Physique\, St Martin d'Hères\, 38402\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260707T110000
DTEND;TZID=Europe/Paris:20260707T120000
DTSTAMP:20260702T132320Z
CREATED:20260702T132320Z
LAST-MODIFIED:20260702T132320Z
UID:10000213-1783422000-1783425600@sfp-alpes.fr
SUMMARY:Jérémie TOPIN (Department of Chemistry\, Université Côte d'Azur\, Nice)
DESCRIPTION:The molecular language of smell : reading odors through receptors\nRésumé : \nThis morning\, you may have enjoyed a cup of coffee or tea and felt that its aroma had stimulated your sense of smell. The volatile molecules in your favourite beverage are recognized by the olfactory receptors (ORs) expressed in your olfactory epithelium. But among your 400 ORs\, which ones were activated by these molecules ?\nTo answer this question\, and more generally to determine the molecular recognition spectrum of ORs\, we design the Molecule to Olfactory Receptor M2OR database\n(https://m2or.chemsensim.fr/)\, which brings together 75\,050 bioassay experiments for 51\,683 distinct OR-molecule pairs.[1] We further combine protein language[2] with graph neural networks to predict OR activation\, and propose a tailored architecture incorporating inductive biases from the protein-molecule interaction.[3] This model outperforms state-of-the-art drug- target interaction prediction models as well as standard GNN baselines. Notably\, our predictions are in agreement with combinatorial coding theory in olfaction. \nReferences\n[1] Lalis\, M.\, Hladiš\, M.\, Khalil\, S. A.\, Briand\, L.\, Fiorucci\, S.\, & Topin\, J\, 2024. M2OR: a database of olfactory receptor–odorant pairs for understanding the molecular mechanisms of olfaction. Nucleic Acids Research\, 52(D1)\, D1370-D1379.\n[2] Elnaggar\, A.\, Heinzinger\, M.\, Dallago\, C.\, Rehawi\, G.\, Wang\, Y.\, Jones\, L.\, … & Rost\, B. (2021). Prottrans: Toward understanding the language of life through self-supervised learning. IEEE transactions on pattern analysis and machine intelligence 2022\, 44(10)\, 7112-7127.\n[3] Hladiš\, M.\, Lalis\, M.\, Fiorucci\, S.\, & Topin\, J. Matching receptor to odorant with protein language and graph neural networks 2023. In The Eleventh International Conference on Learning Representations. \nContact : lucie.sancey@univ-grenoble-alpes.fr ou emmanuel.brun@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/jeremie-topin-department-of-chemistry-universite-cote-dazur-nice/
LOCATION:IAB – Salle de séminaire\, IAB Site Santé - Allée des Alpes\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IAB":MAILTO:appaixfl@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260709T140000
DTEND;TZID=Europe/Paris:20260709T160000
DTSTAMP:20260625T143634Z
CREATED:20260625T143510Z
LAST-MODIFIED:20260625T143634Z
UID:10000208-1783605600-1783612800@sfp-alpes.fr
SUMMARY:Soutenance de thèse par Lorenzo LOMBARDI (CEA-Irig/SyMMES)
DESCRIPTION:Production d’hydrogène à partir de points quantiques par photoélectrolyse de l’eau\nRésumé : \nLes boites quantiques (QD) sont des nanomatériaux semi-conducteurs prometteurs pour la production d’hydrogène par énergie solaire\, grâce à leur forte absorption lumineuse\, leurs coefficients d’extinction élevés et leurs propriétés électroniques modulables. Le développement d’alternatives respectueuses de l’environnement aux QD à base de cadmium est essentiel pour une dissociation de l’eau par voies photocatalytiques et photoélectrochimiques (PEC) durables. Dans ce contexte\, cette thèse étudie les QD à base de CuIn(Ga)S2 pour la production d’hydrogène par photo(électro)lyse de l’eau\, en mettant l’accent sur la relation entre synthèse\, chimie de surface et propriétés optoélectroniques.\nLes travaux explorent d’abord la synthèse organique de QD Cu(In)GaS2 par injection à chaud et chauffage\, combinée à l’ingénierie de l’enveloppe. L’injection à chaud permet d’obtenir des QD CuGaS2/ZnS/ZnS fortement émissifs\, mais des problèmes de purification liés à des résidus de précurseurs sont observés\, limitant la reproductibilité. Les méthodes de chauffage offrent un meilleur contrôle de croissance et une procédure plus simple. Des structures multishell (ZnS\, GaSx\, Al2O3) améliorent la stabilité colloïdale et améliorent les propriétés de photoluminescence. Les positions de bandes sont compatibles avec la production d’hydrogène\, comme confirmé par des analyses électrochimiques et spectroscopiques\, et l’échange de ligands permet le transfert des QD vers des milieux aqueux.\nLa thèse se concentre ensuite sur les synthèses aqueuses (batch\, micro-ondes et flux continu)\, plus durables et facilement scalables. Une nouvelle synthèse hydrothermique assistée par micro-ondes de QD CuInGaS2/GaSx est développée pour étudier l’incorporation du gallium en fonction des ligands. Différents ligands et architectures de surface sont explorés\, montrant un impact marqué sur composition et propriétés optiques. Seuls certains ligands aminocarboxyliques favorisent l’incorporation du gallium\, mise en évidence par spectroscopie d’absorption des rayons X\, tandis que la diffusion neutronique à petit angle fournit des informations structurales complémentaires. La structure électronique est étudiée par voltamétrie cyclique\, XPS\, UPS et PYSA\, corrélant niveaux de bande et performances. Une synthèse en flux continu de QD CuInGaS2 est également mise au point\, démontrant la scalabilité du procédé. Ces approches conduisent à des QD stables présentant des rendements quantiques jusqu’à 20 % et des durées de vie supérieures à 300 ns.\nEnfin\, les performances photocatalytiques et photoélectrochimiques sont évaluées. En photocatalyse\, les QD CuIn(Ga)S2 recouverts de glutathion produisent de l’hydrogène sans cocatalyseur\, tandis que leur association avec des catalyseurs moléculaires permet d’atteindre des TON jusqu’à 12047\, parmi les plus élevés pour des QD sans métaux lourds. En PEC\, des électrodes de TiO2 sensibilisées présentent des photocourants anodiques jusqu’à 1\,45 mA/cm2 à 1\,23 V vs RHE en conditions neutres et sans donneur de trous\, plaçant ces systèmes parmi les plus performants. L’ajout de CoPi entraîne une augmentation modeste du photocourant (5 %) et un décalage cathodique de 0\,2 V\, indiquant que les limitations proviennent surtout des processus de génération\, d’injection et de transport de charge plutôt que de la cinétique catalytique.\nDans l’ensemble\, ce travail démontre le fort potentiel des QD CuIn(Ga)S2 pour la production d’hydrogène durable. Il met en évidence le rôle central de la stratégie de synthèse\, du contrôle de la chimie de surface\, de la gestion des défauts et de l’ingénierie interfaciale pour optimiser les performances photocatalytiques et photoélectrochimiques. Ces résultats fournissent une base solide pour le développement de systèmes à base de QD efficaces et évolutifs pour la conversion de l’énergie solaire en carburants chimiques.​​​​​ \n_ \nContact : alain.farchi@cea.fr
URL:https://sfp-alpes.fr/event/soutenance-de-these-par-lorenzo-lombardi-cea-irig-symmes/
LOCATION:GreEN-ER – Amphi 2A006\, 21 avenue des Martyrs\, Grenoble\, 38000\, France
CATEGORIES:Soutenance,Soutenance de Thèse
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260710T110000
DTEND;TZID=Europe/Paris:20260710T120000
DTSTAMP:20260703T084646Z
CREATED:20260626T134823Z
LAST-MODIFIED:20260703T084646Z
UID:10000211-1783681200-1783684800@sfp-alpes.fr
SUMMARY:Marion JESPERSEN (Department of Microbiology\, Monash University)
DESCRIPTION:Functional and structural insights into O2-adapted hydrogenases\nRésumé : \nHydrogenases are metalloenzymes that catalyse the interconversion of protons and electrons into molecular hydrogen (H2)\, providing valuable models for robust and sustainable H2 catalysts. However\, most characterised hydrogenases are inhibited by oxygen (O2)\, limiting their biotechnological potential. Although diverse [NiFe]- and [FeFe]-hydrogenases have evolved adaptations that support activity\, stability\, or recovery following O2 exposure\, the molecular basis of O2 adaptation remains poorly understood. \nIn this talk\, I will present our ongoing work on O2-adapted hydrogenases from bacteria and archaea inhabiting aerobic soils\, thermoacidophilic environments\, and the gut. By combining physiological\, biochemical\, structural\, and computational approaches\, we investigate how distinct hydrogenase lineages support H2 metabolism under oxygen-exposed conditions.These systems include the high-affinity group 1h [NiFe]-hydrogenase from Mycobacterium smegmatis\, the Sulfolobales clade 2 [NiFe]-hydrogenase from Metallosphaera sedula\, and gut microbial [FeFe]-hydrogenases\, including group B enzymes from Bacteroides species and a group A1 enzyme from Clostridium perfringens. Together\, they highlight the diversity of hydrogenase architectures\, cofactor arrangements\, and electron-transfer strategies that may contribute to O2 resilience. \nOverall\, this work expands the functional and structural repertoire of O2-adapted hydrogenases\, informing our understanding of microbial H2 metabolism and the search for enzymes suited to H2-based biocatalysis. \n_ \nCes séminaires\, ainsi que les soutenances et cours sont ouverts à tous\, notez toutefois que l’accès au campus EPN nécessite un avis de rendez-vous. Merci de remplir ce formulaire et de l’adresser\, plus de 48h à l’avance\, à ce contact. Pensez à vous munir d’une pièce d’identité le jour de votre visite.
URL:https://sfp-alpes.fr/event/marion-jespersen-department-of-microbiology-monash-university/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260720T110000
DTEND;TZID=Europe/Paris:20260720T120000
DTSTAMP:20260703T133346Z
CREATED:20260703T133346Z
LAST-MODIFIED:20260703T133346Z
UID:10000216-1784545200-1784548800@sfp-alpes.fr
SUMMARY:Garry S. HANAN (Département de chimie\, Université de Montréal\, Canada)
DESCRIPTION:Developing New Photosensitizers based on Transition Metal Ions for Green Energy Applications\nRésumé : \nRising global population and increased CO2 levels in the atmosphere have focused attention on developing alternative and widely available carbon-free energy sources (1\,2). Ourresear ch focuses on harnessing the unique properties of excited states in metal complexes to drive self-assembly processes and develop innovative energy applications. By leveraging the photophysical and photochemical behaviors of these complexes\, we explore how light-induced excitations can be utilized to control molecular organization and energy transfer at the nanoscale. The parallels with Natural Photosynthesis are evident: light energy is captured by self-assembled Light Harvesting Complexes and is channeled to a reaction centre which induces electron transfer and the eventual production of chemical energy (3). \nOur approach involves the synthesis of polypyridyl-based metal complexes\, which are known for their stability and tunable electronic properties. By manipulating the excited states of these complexes\, we demonstrate how light can act as a stimulus to induce self-assembly\, leading to the formation of well-defined nanostructures with potential applications in catalysis\, sensing\, and optoelectronics (4). Additionally\, we extend our approach to the development of photoactive molecular devices capable of storing and transferring electrons\, offering insights into the design of next-generation photosensitizers for chemical energy production (5). We have also moved from second- and third-row transition metal ions to the first row\, and explore energy applications of these abundant\, inexpensive and relatively non-toxic metal ions (6). \nReferences\n1. https://ourworldindata.org/world-population-growth (01-05-2026).\n2. https://www.iea.org/world (01-05-2026).\n3. V. Balzani\, A. Credi\, M. Venturi\, Chem Sus Chem 2008\, 1\, 26.\n4. B. Laramée-Milette\, F. Puntoriero\, F. Nastasi\, S. Campagna\, G. S. Hanan\, Chem. Eur. J.\, 2017 23\, 16497.\n5. G. M. Mercier\, E. Rousset\, I. Oubaha\, K. Bandyopadhyay\, A. K. Pal\, I. Ciofini\, L.-M. Chamoreau\, V. Marvaud\, G. S. Hanan\, Chem. Commun. 2025 61 (77)\, 14911-14914.\n6. A. Saha\, G. Turner\, M. Cibian\, S. Serroni\, S. Genovese\, S. Campagna\, G. S. Hanan\, F. Nastasi\, submitted for publication. \nGarry Hanan is professor in the Department of Chemistry at the Université de Montréal\, where he leads the Green Energy Group and is a member of the Centre for Green Chemistry and Catalysis. He earned his B. Sc. from the University of Winnipeg\, Canada\, his PhD from Université Louis Pasteur in Strasbourg\, France\, under the supervision of Jean-Marie Lehn and subsequently conducted postdoctoral studies in Germany with Manfred T. Reetz and in Italy with Vincenzo Balzani and Sebastiano Campagna. Professor Hanan’s research focuses on the design and synthesis of supramolecular photocatalysts capable of harvesting solar energy to drive chemical\ntransformations\, most notably the photoproduction of fuels via water-splitting (producing H₂) and CO₂ reduction.\nHe has received numerous distinctions\, including awards from IUPAC and NSERC\, highlighting his contributions to sustainable chemistry and molecular materials science. He also actively promotes international student exchange. \nContact : frederique.loiseau@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/garry-s-hanan-departement-de-chimie-universite-de-montreal-canada/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
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DTSTART;TZID=Europe/Paris:20260721T140000
DTEND;TZID=Europe/Paris:20260721T150000
DTSTAMP:20260709T121303Z
CREATED:20260709T121303Z
LAST-MODIFIED:20260709T121303Z
UID:10000218-1784642400-1784646000@sfp-alpes.fr
SUMMARY:Ben HUMPHREYS (Institut Laue-Langevin (ILL) Grenoble\, France)
DESCRIPTION:Advancing our Understanding of Responsive Polymer Brushes\nRésumé : \n\nInterfacial properties of a surface can be extensively modified through the addition of a polymer brush layer; a dense array of end-tethered polymers grafted to a surface. When a polymer brush is synthesised with a stimulus responsive polymer\, the surface properties can be tailored to respond\, often reversibly\, to external stimuli such as temperature\, light\, pH\, solvent or electric fields. While these so-called smart materials are particularly promising for high-value applications such as sensors\, nanoactuation and microfluidics\, their response can be significantly influenced by additives such as osmolytes and salts. Unlike untethered polymer systems\, research into the influence of additives for responsive polymer brushes has been sparse\, yet this knowledge is crucial when advancing their utilisation in biomedical and industrial applications. \nThroughout my research career I have primarily focused on the influence of salts and osmolytes on temperature and pH responsive homo- and co-polymer brushes. I will firstly discuss my synthetic methodologies and choice of responsive polymers. This will be followed by a comprehensive outline of the approaches used to investigate these responsive coatings. Here\, starting with the simplest systems\, then gradually increasing complexity\, I have been able to systematically understand the influence of individual additives/changes. This information is invaluable when considering the complex real-world applications that can benefit from the utilisation of smart\, responsive polymer brush surface coatings. \nShort Bio/CV\nIn 2015 I graduated from the University of Newcastle\, Australia\, with a Bachelor of Science\, 1st class honors\, majoring in Chemistry\, followed by my PhD at the same university (2015-2019) titled “Nanostructure of Temperature Responsive Polymer Brushes Modulated by Salt Identity”. I then accepted a post-doc position at Lund University in Sweden\, investigating the internal structural changes of a triglyceride film throughout enzymatic digestion\, with particular focus on the influence of pH and how this influences the species present throughout the lipolytic process. In 2023 I started in my current position as instrument responsible for the D17 neutron reflectometer at the ILL where I have re-established my research on responsive polymer brushes with a focus on osmolyte and salt additives in aqueous solutions. \n_ \nContact : deborah.verger@grenoble-inp.fr
URL:https://sfp-alpes.fr/event/ben-humphreys-institut-laue-langevin-ill-grenoble-france/
LOCATION:LMGP – salle des séminaires\, Grenoble INP -Phelma 3 parvis Louis Néel\, Grenoble\, 38054\, France
CATEGORIES:Séminaire
ORGANIZER;CN="LMGP":MAILTO:deborah.verger@grenoble-inp.fr
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