• Bienvenue au DCM


    Le Département de Chimie Moléculaire de Grenoble est une unité mixte de recherche (UMR-5250) associant le CNRS et l’Université Grenoble Alpes. Créé le 01 Janvier 2007 par le regroupement des unités LEDSS (UMR-5616) et LEOPR (UMR-5630), le DCM mobilise environ 150 personnes autour de deux axes de recherches interactifs qui sont la chimie pour la santé et la chimie pour les nanosciences.

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  • BioCEN

    Bioélectrochimie pour les capteurs, l’énergie et les nanomatériaux

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  • I2BM

    Ingénierie et Interactions BioMoléculaires

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  • Chimie Inorganique Redox

    CIRE laboratory develops its research in the fields of molecular electrochemistry and redox photochemistry. We design molecular architectures with diverse functionalities often inspired by a bio-mimetic approach. Our work is directed towards both fundamental research(switchable systems, artificial photosynthesis, metal-radical coupling) and practical applications (nano-chemical devices, inhibitors development).

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  • SeRCO

    Synthèse et Réactivité en Chimie Organique

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  • Spectrométrie, Interactions, Chimie Théorique

    Expertise in the field of theoretical chemistry and experimental mass spectrometry :
    At the upper right, study of alkynes activation by Au(I) complexes with the help of Mass spectrometry; At the bottom in the left, TD-DFT development for the photochemistry ; At the bottom in the middle QM/MM Studies of Tyrosinase inhibitors ; At the right modelization of the reactivity in solution 

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Agenda

ZOOM

ZOOM Negative SPR Signals during Low Molecular Weight Analyte Recognition
Surface plasmon resonance (SPR) is a powerful technique for studying biomolecular interactions mainly due to its sensitivity and real-time and label free advantages. While SPR signals are usually positive, only a few studies have reported sensorgrams with negative signals. The aim of the present work is to investigate and to explain the observation of negative SPR signals with the hypothesis that it reflects major changes in ligand conformation resulting from target binding. We demonstrated that these negative unconventional signals were due to the negative complex (ligand/analyte) refractive index increment (RII) deviation from the sum of the RII of the individual entities which counterbalanced the theoretical increase of the signal triggered by the target recognition and the ligand folding. We also found that the conformation change of biomolecules can induce a negative or a positive complex RII deviation depending on its sequence and immobilization mode.
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