Academic literature on the topic 'Protéines, structures secondaires'
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Journal articles on the topic "Protéines, structures secondaires"
Okoroafor, O. N., P. C. Animoke, B. M. Anene, et al. "Constraints and prospects of turkey production in Enugu state south-eastern Nigeria." Nigerian Journal of Animal Production 47, no. 5 (2020): 142–55. http://dx.doi.org/10.51791/njap.v47i5.1328.
Full textDissertations / Theses on the topic "Protéines, structures secondaires"
Levin, Jonathan Mark. "Prédiction de la structure des protéines par homologie : structures secondaires et modélisation de la structure tertiaire." Paris 11, 1989. http://www.theses.fr/1989PA112135.
Full textBograh, Alfred. "Effets des anions inorganiques, des polyamines, et du cholestérol sur les structures secondaires des protéines du photosystème II." Thèse, Université du Québec à Trois-Rivières, 1998. http://depot-e.uqtr.ca/4743/1/000642364.pdf.
Full textEudes, Richard. "Développements méthodologiques relatifs à l'attribution et à la prédiction des structures secondaires des protéines globulaires : classification structurale de mutations du transporteur CFTR, observées chez des patients atteints de mucoviscidose." Paris 6, 2006. http://www.theses.fr/2006PA066170.
Full textPaulet, Damien. "Variation d'hydrophobicité et structure secondaire des protéines transmembranaires." Thesis, Montpellier 1, 2010. http://www.theses.fr/2010MON13518/document.
Full textBackground. Few high-resolution structures of integral membranes proteins are available, as crystallization of such proteins needs yet to overcome too many technical limitations. Nevertheless, prediction oftheir transmembrane (TM) structure by bioinformatics tools provides interesting insights on the topology of these proteins.Method. We describe here how to extract new information from the analysis of hydrophobicity variations or hydrophobic pulses (HPulses) in the sequence of integral membrane proteins using the Hydrophobic Pulse Predictor, a new tool we developed for this purpose. To analyze the primary sequence of 70 integralmembrane proteins we defined two levels of analysis : G1-HPulses for sliding windows of n=2 to 6 andG2-HPulses for sliding windows of n=12 to 16.Results. The G2-HPulse analysis of 541 transmembrane helices allowed the definition of the new conceptof transmembrane unit (TMU) that groups together transmembrane helices and segments with potentialadjacent structures. In addition, the G1-HPulse analysis identified helix irregularities that correspondedto kinks, partial helices or unannotated structural events. These irregularities could represent key dynamicelements that are alternatively activated depending on the channel status as illustrated by the crystalstructures of the lactose permease in different conformations. Our results open a new way in the understanding of transmembrane secondary structures : hydrophobicity through hydrophobic pulses stronglyimpacts on such embedded structures and is not confined to define the transmembrane status of aminoacids
Gibrat, Jean-François. "Modélisation sur calculateur électronique de la structure tridimensionnelle des protéines." Paris 6, 1986. http://www.theses.fr/1986PA066471.
Full textTran, Van-Du Thuong. "Modélisation et prédictionde la structure super-secondaire des protéines transmembranaires canaux-beta." Palaiseau, Ecole polytechnique, 2011. http://www.theses.fr/2011EPXX0104.
Full textTran, Thuong Van Du. "Modélisation et prédiction de la structure super-secondaire des protéines transmembranaires canaux-beta." Phd thesis, Ecole Polytechnique X, 2011. http://pastel.archives-ouvertes.fr/pastel-00711285.
Full textMiroux, Bruno. "Analyse de la structure secondaire d'une protéine membranaire mitochondriale la protéine découplante du tissu adipeux brun." Paris 11, 1993. http://www.theses.fr/1993PA11T018.
Full textRomanet, Patrick. "Prédiction de la structure secondaire des protéines par analyse spectrale de la séquence d'hydrophobicité." Grenoble 1, 1999. http://www.theses.fr/1999GRE10139.
Full textMurail, Samuel. "Mécanismes moléculaires des interactions ligand-protéine membranaire : étude biophysique d'un récepteur couplé aux protéines G, VPAC1, et du récepteur périphérique des benzodiazépines." Paris 7, 2008. http://www.theses.fr/2008PA077120.
Full textThe main goal of this work has been to contribute to elucidate the molecular mechanism underlying protein-ligand interaction within the membrane. The first protein studied is the peripheral benzodiazepine receptor (PBR) and its ligand interest, cholesterol. PBR is involved in steroid biosynthesis, through the cholesterol translocation from the outer to the inner membrane of mitochondria. In the absence of any available structural information on PBR, our first work has been to focus on the PBR structure, by determining from NMR data the conformation of synthetic fragments encompassing the predicted transmembrane domains and then by studying the entire recombinant protein by NMR and circular dichroism. In second step, several studies combining mutagenesis and molecular modeling have be performed which allow to characterize PBR-cholesterol interaction, and the role of key residues this interaction. The second part of our work is devoted to study the interaction of the extracellular domain VPAC1, a G-protein coupled receptor, with the vasointestinal neuropeptide (VIP), which plays important role in human physiopathology. From the VIP conformation obtained by NMR a photoaffinity data, we were able to propose a molecular model of the VIP-VPAC1 interaction using docking protocols and to characterize this interaction using molecular dynamics simulation. Our result contributes to elucidate the molecular basis of VIP recognition and more generally understand the ligand-receptor interaction process of the class B family of GPCRs
Book chapters on the topic "Protéines, structures secondaires"
"3 La structure secondaire." In La structure des protéines. EDP Sciences, 2020. http://dx.doi.org/10.1051/978-2-7598-2243-0-006.
Full text"3 La structure secondaire." In La structure des protéines. EDP Sciences, 2020. http://dx.doi.org/10.1051/978-2-7598-2243-0.c006.
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