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Academic literature on the topic 'Conformation des protéines'
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Journal articles on the topic "Conformation des protéines"
Reiter, Eric. "Mécanismes d’action et rôles multiples des β-arrestines dans la biologie des récepteurs couplés aux protéines G." Biologie Aujourd’hui 215, no. 3-4 (2021): 107–18. http://dx.doi.org/10.1051/jbio/2021010.
Full textCrine, P., N. Antoine, and J. Beaudet. "La conformation des protéines lors de leur translocation dans les membranes biologiques." médecine/sciences 5, no. 9 (1989): 678. http://dx.doi.org/10.4267/10608/4044.
Full textK. A., Badmus, Kabir M., Adeyinka I. A., Adeleke R. A., Iyiola-Tunji A. O., Tijani A. A., and Akinsola O. M. "Short term selection response on growth and reproductive traits in broiler lines of chicken." Nigerian Journal of Animal Production 50, no. 2 (February 28, 2024): 51–65. http://dx.doi.org/10.51791/njap.v50i2.3961.
Full textBerto, Ludovic, Anaëlle Dumazer, Fanny Malhaire, Giuseppe Cannone, Vinothkumar Kutti Ragunath, Cyril Goudet, and Guillaume Lebon. "Les avancées récentes dans le domaine de la biologie structurale des récepteurs couplés aux protéines G de la classe C : Le récepteur métabotropique du glutamate 5." Biologie Aujourd’hui 215, no. 3-4 (2021): 85–94. http://dx.doi.org/10.1051/jbio/2021013.
Full textGarnier, J. "Simulation de la conformation des peptides et des protéines : dévéveloppement de nouveaux polypeptides biologiquement actifs." Journal de Chimie Physique 82 (1985): 591–98. http://dx.doi.org/10.1051/jcp/1985820591.
Full textLEPAGE, C., H. RABESONA, S. KOZIN, A. BLOND, T. HAERTLE, P. DEBEY, and S. REBUFFAT. "Approche physicochimique de la structure de la protéine prion PrPc : Plasticité conformationnelle de peptides de la région 121-170 (H1-S2) de la protéine prion ovine." INRAE Productions Animales 17, HS (December 20, 2004): 39–44. http://dx.doi.org/10.20870/productions-animales.2004.17.hs.3624.
Full textHENRY, Y. "Alimentation du porc pour la production de viande maigre : évolutions récentes et perspectives." INRAE Productions Animales 6, no. 1 (February 27, 1993): 31–45. http://dx.doi.org/10.20870/productions-animales.1993.6.1.4185.
Full textMéplan, Catherine, Gerald Verhaegh, Marie-Jeanne Richard, and Pierre Hainaut. "Metal ions as regulators of the conformation and function of the tumour suppressor protein p53: implications for carcinogenesis." Proceedings of the Nutrition Society 58, no. 3 (August 1999): 565–71. http://dx.doi.org/10.1017/s0029665199000749.
Full textAnago, Eugénie, Guilphados Djogbede, Ezéchiel Mahougnon Salomon Fiogbe, Gaétan Augustin Julien Segbo, and Dèwanou Casimir Akpovi. "Rôle de la glycation des protéines dans les complications et la thérapie du diabète: revue bibliographique." International Journal of Biological and Chemical Sciences 16, no. 6 (March 12, 2023): 2930–44. http://dx.doi.org/10.4314/ijbcs.v16i6.37.
Full textMohd Jaafar, F., H. Attoui, X. W. Li, O. Alpar, and P. P. C. Mertens. "Expression des protéines VP2 et VP5 de la capside externe du virus de la fièvre catarrhale ovine." Revue d’élevage et de médecine vétérinaire des pays tropicaux 62, no. 2-4 (February 1, 2009): 173. http://dx.doi.org/10.19182/remvt.10076.
Full textDissertations / Theses on the topic "Conformation des protéines"
Le, Cam Eric. "Conformation de l'ADN et interactions ADN-protéines en microscopie électronique." Paris 11, 1995. http://www.theses.fr/1995PA11T007.
Full textJambon, Martin. "Un système bioinformatique de recherche de similitudes fonctionnelles dans les structures 3D de protéines." Lyon 1, 2003. http://www.theses.fr/2003LYO10075.
Full textBouthinon, Dominique. "Apprentissage à partir d'exemples ambigus : étude théorique et application à la découverte de structures communes à un ensemble de séquences d'ARN." Paris 13, 1996. http://www.theses.fr/1996PA132033.
Full textFlahaut, Christophe. "Modifications post-traductionnelles et conformation des chaînes lourdes de l'inter-alpha-inhibiteur." Lille 1, 2000. https://pepite-depot.univ-lille.fr/LIBRE/Th_Num/2000/50376-2000-73.pdf.
Full textYun, Mi-Ran. "Echantillonnage des petits et grands déplacements atomiques dans les protéines et complexes moléculaires." Paris 7, 2007. http://www.theses.fr/2007PA077128.
Full textThe knowledge of protein conformational space is a major importance in biology, while protein binding (beyond of the notion "lock and key" the conformational changes play an important role. The several experimental (NMR, X-ray crystallography. . . ) and theoretical studies (Molecular Dynamics, Monte Carlo method. . . ), are used for describe molecular conformational space. The side chain flexibility is well characterized, however main chain flexibility rest in problem. We propose an activated method, ARTIST (Activation-Relaxation Technique for Internal coordinate Space Trajectories) fused and adapted from two programs, (ART and LIGAND) capable to sample, in internal coordinates, local or collective displacements on proteins involving protein backbone. We show the capacity of ARTIST to sample conformational changes from small proteins to complexes using AMBER and FLEX ail atom force fields. The ARTIST is adapted with the coarse-grained force field (OPEP), first tests were performed on a small protein
Liebschner, Dorothée. "Propriétés électrostatiques et structurales des protéines diffractant à haute résolution." Thesis, Nancy 1, 2010. http://www.theses.fr/2010NAN10085/document.
Full textThis study is about the electrostatic and structural properties of proteins diffracting at high X-ray resolution. Two different aspects are tackled which are 1) the analysis of properties derived from their charge distribution, parting from a fundamental point of view and 2) the application of methods used in high resolution macromolecular crystallography to two enzymes of major interest.After the analysis of the structure and electrostatic properties of PfluDING protein, the binding mode of a phosphate ion, located in the active site, was elucidated at two different pH values. Particularly, this study demonstrates that a diffuse hydrogen bond assures the protonation state of the phosphate ion, which is thus identical at each pH value. The second enzyme studied is the proteine DFPase which is capable of hydrolysing nerve agents. A high resolution X-ray structure and a medium resolution neutron structure where compared. The analysis points out the differences between the two models and a new catalytic mechanism could be proposed.The more fundamental aspects of this study are about the secondary structural elements of proteins: their electrostatic properties in terms of electrostatic moments (dipole and quadrupole moments of helices and sheets) as well as the hydrogen bond network assuring the cohesion of helices have been analyzed. It has been shown that certain interactions between peptide units within helices, represented usually as hydrogen bonds, should actually be considered as pure electrostatic contacts
Joseph, Agnel Praveen. "Comparison of protein folds based on similarities in local backbone conformation." Paris 7, 2011. http://www.theses.fr/2011PA077100.
Full textProtein Structure Comparison is an efficient means for function characterization and evolutionary studies. We propose an improved approach for three dimensional (3D) protein structure comparison based on similarities in local backbone conformations. A library of 16 frequently occurring penta-peptide backbone conformations, namely Protein Blocks (1,2), was used to transform 3D structural information as a sequence. This reduces the problem of structural comparison to a more classical sequence alignment. The use of an anchor based dynamic programming algorithm with specialized gap penalties resulted in a significant improvement over earlier studies based on simple global alignments. The alignment quality improved by about 82% and the efficiency in searching a structure databank for related folds was also enhanced by 6. 2% (3,4). This approach for pairwise structure comparison (iPBA) is implemented as a web server http://www. Dsimb. Inserm. Fr/dsimb tools/ipba/. IPBA was further extended to the development of a multiple structural alignment tool. A progressive alignment strategy was adopted and local weights were added for structurally similar regions (mulPBA) (Joseph et al. In peparation). Comparison with other structural alignment tools showed that both the PB based alignment approaches (iPBA & mulPBA) often give the best performance and can be placed as one of the top two methods currently available. Local conformational variations among structurally similar proteins were also studied in detail (Joseph et al. Submitted). Subtle changes are found to occur mainly in the regions comprising turns. The preference for the indel sites are also confined to a few backbone conformations involving p-turns and helix C-caps. The alignment strategy behind iPBA was also used to assess the performance of a fold recognition approach based on PB prediction. The influence of species specific data on sequence-structure relationships was also analyzed using PBs (5). Relationships observed in chameleon sequences (6) that adopt different conformations in protein structures, was studied in detail. An efficient protocol for the assignment of PolyProline-II helices, which can be easily incorporated into the DSSP secondary structure assignment tool was also developed (7)
Gibrat, Gabriel. "Structure et dynamique de l'état natif et des états dénaturés par la chaleur et la pression de la calmoduline : une étude par diffusion de neutrons et spectroscopies optiques." Paris 11, 2007. http://www.theses.fr/2007PA112297.
Full textThis thesis work is concerned with the study of thermal and pressure denaturation of calmodulin, a small (16 kDa), monomeric, soluble, and “mainly α” calci-protein. This protein, that is an excellent model system for unfolding/folding studies, exists in two forms: the holo and the apo forms, depending on the presence or the absence of calcium ions. The comparison of thermal and pressure unfolding pathways shows clearly that the unfolding of both calmodulin forms cannot be correctly described using a “two-state” model (Native Unfolded). The stabilities given by pressure unfolding experiments and by thermal unfolding ones are largely different, signing the presence of intermediate states. Even if thermal unfolding pathway does not exhibit “molten-globule” intermediate state, classically encountered in protein unfolding pathways, pressure unfolding pathways of both calmodulin forms contain compact intermediate state, with a maximum population around 3000 bar. Up to this pressure, the pressure behaviours of the two calmodulin forms are asymmetric: the domains of the holo form are compacted under pressure, while those of the apo form are dilated. The conformation of the final state of thermal unfolding of apo-calmodulin is similar to that of a Gaussian chain, with some residual secondary structures. Its dynamics looks more heterogeneous than that of the native state, suggesting that the distance of atom to protein backbone plays a more important role than the solvent exposure to the residue. An important finding is that the thermal unfolding of apo-calmodulin is irreversible. The last part of this thesis deals with the unfolding of a more complex oligomeric system: the C-phycocyanin photosynthetic protein. The unfolding pathway of this protein contains several steps, including firstly the oligomer dissociation, and secondly the unfolding of the dissociated monomer. This unfolding mechanism is out of equilibrium at the time-scale of classical experimentation
Talansier, Émeline. "Étude du foisonnement par mélangeur statique appliqué à la structuration des mousses de blanc d'oeuf dénaturé par traitement thermique." Nantes, 2009. http://www.theses.fr/2009NANT2009.
Full textEgg white proteins (EWP) are widely used in food industries because of their excellent foaming properties. The pasteurization is often performed in the dry state to prevent a damage of their functional properties. The aim of this study is to estimate the effect of dry heat treatment at different levels on the EWP foams properties. The conformational changes of proteins and the formation of soluble aggregates caused by the treatment are investigated in relation to interfacial properties. A link is explored between the EWP denaturation and foam characteristics. As a first approach, foams are processed with a standard home mixer. A link is established between interfacial and rheological properties of foams, and foam stability improved for mild treatments. But such batch foaming process does not allow the production of fixed overrun or bubble size distribution. The static mixer (Sulzer-SMX10™) is therefore required to control the foam structure. It is then possible to link foams properties, i. E. Texture and stability, to their structural parameters (void fraction and bubbles size). The effect of the protein denaturation induced by dry heat treatment is also quantified. The SMX10™ static mixer may be proposed as an eminent alternative process to produce foams at lab but mostly at an industrial scale. An axial physical 1D model is proposed, based on the calculations along the mixer of the pressure drop and the bubble size. The gas expansion is taken into account, and a semi-empirical model is used to characterise the foam viscosity. This approach makes scale-up possible, in the view to use this process for a large range of scales and applications
Rousseau, Marie-Ève. "Étude de la conformation et de l'orientation des protéines dans les soies naturelles." Thesis, Université Laval, 2007. http://www.theses.ulaval.ca/2007/24312/24312.pdf.
Full textBooks on the topic "Conformation des protéines"
M, Thornton Janet, ed. Atlas of protein side-chain interactions. Oxford: IRL Press at Oxford University Press, 1992.
Find full textSingh, Juswinder. Atlas of protein side-chain interactions. Oxford: IRL Press at Oxford University Press, 1992.
Find full textMichael, Sundstrom, Norin Martin, and Edwards Aled, eds. Structural genomics and high throughput structural biology. Boca Raton, FL: Taylor&Francis, 2006.
Find full textT, Mant Colin, and Hodges Robert S, eds. High-performance liquid chromatography of peptides and proteins: Separation, analysis, and conformation. Boca Raton: CRC Press, 1991.
Find full textAndrás, Aszódi, ed. Protein geometry, classification, topology and symmetry: A computational analysis of structure. Bristol: Institute of Physics Pub., 2005.
Find full textH, Lundstrom Kenneth, ed. Structural genomics on membrane proteins. Boca Raton: Taylor & Francis, 2006.
Find full textM, Kazmierski Wieslaw, ed. Peptidomimetics protocols. Totowa, NJ: Humana Press, 1999.
Find full textHenrik, Bohr, and Brunak Søren, eds. Protein folds: A distance-based approach. Boca Raton: CRC Press, 1996.
Find full text1948-, Walker John M., ed. The protein protocols handbook. 2nd ed. Totowa, N.J: Humana Press, 2002.
Find full textI, Chasman Daniel, ed. Protein structure: Determination, analysis, and applications for drug discovery. New York: Marcel Dekker, 2003.
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