About: Michel Marraud

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About: Michel Marraud Goto Sponge NotDistinct Permalink

An Entity of Type : foaf:Person, within Data Space : data.idref.fr associated with source document(s)

Attributes	Values
type	Person
sameAs	Marraud, Michel Marraud, Michel Marraud, Michel
bnf-onto:FRBNF	12189680(xsd:integer)
preferred label	Marraud, Michel
name	Michel Marraud
dbpedia-owl:citizenship	http://sws.geonames.org/3017382/
Language	http://lexvo.org/id/iso639-3/fra
Given name	Michel
familyName	Marraud
has biographical i...tion (Deprecated)	Chercheur au Laboratoire de chimie physique macromoléculaire de l'École nationale supérieure des industries chimiques de Nancy (UA 494 du CNRS) (en 1989)
gender	male
is sameAs of	Marraud, Michel Marraud, Michel
is Thesis advisor of	http://www.sudoc.fr/044112432/id http://www.sudoc.fr/043661475/id http://www.sudoc.fr/043767877/id http://www.sudoc.fr/043998577/id http://www.sudoc.fr/043748856/id http://www.sudoc.fr/044215436/id http://www.sudoc.fr/043980554/id http://www.sudoc.fr/044152868/id http://www.sudoc.fr/044104987/id Synthèse et analyse structurale de n-hydroxy peptides Synthèse et structure des peptides réduits, influence structurale de l'état aminé ou ammonium du lien amidé réduit http://www.sudoc.fr/245704779/id http://www.sudoc.fr/246246421/id http://www.sudoc.fr/246258314/id http://www.sudoc.fr/246398701/id http://www.sudoc.fr/259529702/id Synthèse et analyse conformationnelle de tripeptides dérivés de la séquence signal Asn-Xxx-Ser codant pour la N-glycosylation des protéines http://www.sudoc.fr/246328002/id Etude spectroscopique de l'état d'hydratation de peptides en milieu micellaire biomimétique, application au tripeptide chimiotactique Repliements induits par l'asparagine et l'acide aspartique dans les peptides http://www.sudoc.fr/245762744/id Rétropeptides, modulations conformationnelles par inversion de la liaison amide, application à la leucine-enképhaline Étude d'un décapeptide à activité de type benzodiazépine issu d'une protéine du lait bovin
is Praeses of	http://www.sudoc.fr/043661068/id http://www.sudoc.fr/245704507/id Modélisation des interactions anticorps-antigène, application à une maladie auto-immune, la myasthénie
is Author of	http://www.sudoc.fr/004724062/id Solution structures of the fibronectin-like Leishmania gp63 SRYD-containing sequence in the free and antibody-bound states--transferred NOE and molecular dynamics studies The third-dimensional structure of the complex between an Fv antibody fragment and an analogue of the main immunogenic region of the acetylcholine receptor: a combined two-dimensional NMR, homology, and molecular modeling approach. Structural Investigation of “cis” and “trans” Vinylogous Peptides: cis-Vinylog Turn in Folded cis-Vinylogous Peptides, an ExcellentMimic of the Natural β-Turn Phosphorus-31 Nuclear Magnetic Resonance Studies on Coenzyme Binding and Specificity in Glyceraldehyde-3-Phosphate Dehydrogenase † Structural and conformational study of the aluminum-thymulin complex using 1-D and 2-D NMR techniques Synthesis and conformational analysis of AzAsx-containing oligopeptides Solution structure of an SRYD-containing sequence (250-257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamics .beta.I and .beta.II-turn conformations in model dipeptides with the Pro-Xaa sequences Conformational perturbations induced by N-amination and N-hydroxylation of peptides Solvation state of the Tyr side chain in peptides. An FT-IR and 17O NMR approach Influence of Side Chain Restriction and NH···π Interaction on theβ-Turn Folding Modes of Dipeptides Incorporating PhenylalanineCyclohexane Derivatives Influence of Silaproline on Peptide Conformation andBioactivity Two-Dimensional1H-nmr study of antigen-antibody interactions: Binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody Conformational and antigenic properties of SRYD-containing peptide analogues of Leishmania gp63 adhesion site Involvement of side functions in peptide structures: the Asx turn. Occurrence and conformational aspects Experimental Calibration of a Karplus Relationship in Order to Study the Conformations of Peptides by Nuclear Magnetic Resonance Structural Investigation of “cis” and “trans” Vinylogous Peptides: cis-Vinylog Turn in Folded cis-Vinylogous Peptides, an Excellent Mimic of the Natural β-Turn Synthesis and conformational analysis of AzAsx-containing oligopeptides Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide Synthesis and Structure of Symmetrical Bicyclic Hexapeptides Bridged by Metathesis Reaction The main immunogenic region (MIR) of the nicotinic acetylcholine receptor and the anti-MIR antibodies Structural elucidation of the b-turn inducing (S)-[3-amino-4-oxo-2,3-dihydro-5H-benzo[b][1,4]thiazepin-5-yl] acetic acid (DBT) Crystal structure of diacetylhydrazino analog of the valine residue Structure of epitopes recognized by the antibodies to α(181–192) peptides of neuronal nicotinic acetylcholine receptors: extrapolation to the structure of acetylcholine-binding domain
is primary topic of	http://www.idref.fr/030493501
is Publishing director of	http://www.sudoc.fr/001442724/id

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