M. H. Baron

Université Grenoble Alpes

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F. Fillaux

Sorbonne Université

C. de Lozé

Centre National de la Recherche Scientifique

Gordon J. Kearley

University College Dublin

L. Grajcar

Centre National de la Recherche Scientifique

Mahmoud Ghomi

Instituto de Estructura de la Materia

Sophie Lecomte

Institut Polytechnique de Bordeaux

J. Tomkinson

Rutherford Appleton Laboratory

G. Berthier

Centre de Gestion Scientifique

A. Aamouche

Cadi Ayyad University

H. Jobic

Institut de Recherches sur la Catalyse et l'Environnement de Lyon

Cooperative Institutions

Centre National de la Recherche Scientifique

Sorbonne Université

Université Paris Cité

Laboratoire de Spectroscopie pour les Interactions, la Réactivité et l'Environnement

University of Turin

Laboratoire de Réactivité de Surface

Université Grenoble Alpes

Laboratoire de Chimie Physique

Université de Toulouse

Commissariat à l'Énergie Atomique et aux Énergies Alternatives

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Étude par spectrométrie de vibration des interactions entre les amides et les sels

Journal de Chimie Physique (1972)

M. H. Baron C. de Lozé

Les interactions amide-sels sont étudiées, par spectrométrie de vibration, en solution ternaire dans deux solvants organiques (CH3CN et THF) et en mélange binaire. Les amides utilises sont le N,N-dimethyl et le N-méthyl acétamide; les sels, des perchlorates, des halogénures de tétrabutylammonium et le bromure de lithium. L'évolution de la bande Li+-cage montre que ce cation est solvate par l'amide. Les différentes espèces amide-sel formées sont identifiées par le comportement des vibrateurs νCO (pour le DMA), amide I, amide II, νNH (pour le NMA). Le groupement carboxyle des amides peut fixer un ou deux calions, ou un cation et un groupement NH, les groupements NH fixent les allions. Les répercussions de ces fixations sur l'état des groupements OCN et OCNH sont discutées.

Amide

10.1051/jcp/1972691084

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Citations (15)

FTIR and 2D-FTIR spectroscopic study of cytochrome c 552 adsorbed on anionic and hydrophobic surfaces

Springer eBooks (1999)

Sophie Lecomte Christophe Hilleriteau J. P. Forgerit M. Revault M. H. Baron

Thermus thermophilus

Cytochrome C1

Hydrophobic effect

Cytochrome P450 reductase

10.1007/978-94-011-4479-7_40

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Doppler broadening measurements in FRX-C/LSM

OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (1989)

M. H. Baron R. E. Chrien

Measurements obtained in situ during field reversed configuration (FRC) formation show that the Doppler broadening ion temperature T{sub CV} is larger by a factor of two or more than the ion temperature T{sub i} derived from pressure balance and Thomson scattering. After a time comparable to an ion-ion equilibrium time, T{sub CV} and T{sub i} come into agreement with each other. An exception to this picture occurs in the lowest fill pressure condition (2 mtorr), for which T{sub CV} > T{sub i} is maintained throughout the FRC lifetime. Earlier Doppler broadening measurements in FRX-B and FRX-C also showed persistent, anomalously high T{sub CV} at low fill pressure. The initially high values of T{sub CV} are probably caused by convective motion generated by the radial implosion. The low fill pressure results suggest an enhanced ohmic power input to the carbon ions. 7 refs., 3 figs.

Implosion

Source

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Supplementary material to "SnowPappus v1.0, a blowing-snow model for large-scale applications of Crocus snow scheme" : Pleiades snow depth maps analysis

Zenodo (CERN European Organization for Nuclear Research) (2023)

M. H. Baron

This Folder contains : - necessary codes to reprduce Fig. 5, 12 and 13 of the third version of the submitted manuscript SnowPappus v1.0, a blowing-snow model for large-scale applications of Crocus snow scheme" - necessary data to run these codes, including extracts of simulation outputs - A readme.txt which explains how to run everything

Pleiades

Crocus

10.5281/zenodo.10204742

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Enzyme Adsorption on Soil Mineral Surfaces and Consequences for the Catalytic Activity

Books in soils, plants, and the environment (2002)

Hervé Quiquampoix S. Servagent-Noinville M. H. Baron

Soil enzyme

10.1201/9780203904039.ch11

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Citations (61)

Etude spectroscopique de derives mercuriques d'amidesthiols

Journal of Molecular Structure (1984)

C. Perchard M. H. Baron C. de Lozé

Mercury

Carboxylate

10.1016/0022-2860(84)85067-x

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Citations (7)

ChemInform Abstract: PRERESONANCE RAMAN SPECTRA OF TYROSINE AND IODOTYROSINE AT PH 1 AND 11.5

Chemischer Informationsdienst (1984)

M. H. Baron C. de Lozé T. Mejean M.J. Coulange P. Y. Turpin

10.1002/chin.198415044

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Spectroscopic Investigation of the Interaction Between Xenobiotic Substrates and Clay Materials

Springer eBooks (1993)

A. Vimond-Laboudigue R. Prost M. H. Baron J. Merlin

10.1007/978-94-011-1934-4_132

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Structure in solution of protected homo‐oligopeptides of L‐valine, L‐isoleucine, and L‐phenylalanine: An infrared absorption study

Biopolymers (1978)

M. H. Baron C. de Lozé Claudio Toniolo Gerald D. Fasman

Abstract Monodisperesed, N‐and C‐Protected homo‐oligopeptides [number ( n ) of resides from 2 to 5] of L ‐valine, L ‐isoleucine, and L ‐phenylalnine were studied by ir absorption spectroscopy between 1200 and 350 cm −1 at various solvents. The solvents and chain‐length effects were examined for non‐hydrogen‐bonded peptide groups. The frequencies of the self‐associated species are consistent with a model derived from the amide data. Self‐association species are consistent with a model derived from the amide data. Self‐association is favored by higher values of n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain soluble. For n = 2, the peptide is insoluble when more than two chains are bonded. For n = 3, 4, several chains may be associated by sliding along one another and remain slouble. For n = 5, the effect of n is to favour a model in which two chains exactly face each other so that the peptide precipitates at relatively low concentration.

Isoleucine

Amide

Oligopeptide

Side chain

Tripeptide

10.1002/bip.1978.360170915

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Citations (62)

Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis

Journal of Colloid and Interface Science (1999)

M. H. Baron M. Revault S. Servagent-Noinville J. Abadie Hervé Quiquampoix

Residue (chemistry)

10.1006/jcis.1999.6189

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Citations (122)