Academic literature on the topic 'Hélice polyproline de type II'

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Journal articles on the topic "Hélice polyproline de type II"

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Zagrovic, B., J. Lipfert, E. J. Sorin, et al. "Unusual compactness of a polyproline type II structure." Proceedings of the National Academy of Sciences 102, no. 33 (2005): 11698–703. http://dx.doi.org/10.1073/pnas.0409693102.

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van Holst, G. J., S. R. Martin, A. K. Allen, D. Ashford, N. N. Desai, and A. Neuberger. "Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism." Biochemical Journal 233, no. 3 (1986): 731–36. http://dx.doi.org/10.1042/bj2330731.

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The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a hydroxyproline-rich glycopeptide and its deglycosylated derivative. It is concluded that the lectin contains about 35% polyproline II conformation, 34% type II beta-turn and 31% irregular conformation. No indications were found for the presence of alpha-helix or beta-sheet conformations. The polyproline II conformati
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Kubyshkin, Vladimir, and Nediljko Budisa. "Construction of a polyproline structure with hydrophobic exterior using octahydroindole-2-carboxylic acid." Organic & Biomolecular Chemistry 15, no. 3 (2017): 619–27. http://dx.doi.org/10.1039/c6ob02306a.

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Lam, Sik Lok, and Victor L. Hsu. "NMR identification of left-handed polyproline type II helices." Biopolymers 69, no. 2 (2003): 270–81. http://dx.doi.org/10.1002/bip.10354.

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Song, Jikui, Jered V. McGivern, Karl W. Nichols, John L. Markley, and Michael D. Sheets. "Structural basis for RNA recognition by a type II poly(A)-binding protein." Proceedings of the National Academy of Sciences 105, no. 40 (2008): 15317–22. http://dx.doi.org/10.1073/pnas.0801274105.

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We identified a functional domain (XlePABP2-TRP) of Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2). The NMR structure of XlePABP2-TRP revealed that the protein is a homodimer formed by the antiparallel association of β-strands from the single RNA recognition motif (RRM) domain of each subunit. In each subunit of the homodimer, the canonical RNA recognition site is occluded by a polyproline motif. Upon poly(A) binding, XlePABP2-TRP undergoes a dimer-monomer transition that removes the polyproline motif from the RNA recognition site and allows it to be replaced by the adenos
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Vlasov, Peter K., Anna V. Vlasova, Vladimir G. Tumanyan, and Natalia G. Esipova. "A tetrapeptide-based method for polyproline II-type secondary structure prediction." Proteins: Structure, Function, and Bioinformatics 61, no. 4 (2005): 763–68. http://dx.doi.org/10.1002/prot.20670.

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Doose, S., H. Neuweiler, H. Barsch, and M. Sauer. "Probing polyproline structure and dynamics by photoinduced electron transfer provides evidence for deviations from a regular polyproline type II helix." Proceedings of the National Academy of Sciences 104, no. 44 (2007): 17400–17405. http://dx.doi.org/10.1073/pnas.0705605104.

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Srinivasan, Mythily, and A. Keith Dunker. "Proline Rich Motifs as Drug Targets in Immune Mediated Disorders." International Journal of Peptides 2012 (May 16, 2012): 1–14. http://dx.doi.org/10.1155/2012/634769.

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The current version of the human immunome network consists of nearly 1400 interactions involving approximately 600 proteins. Intermolecular interactions mediated by proline-rich motifs (PRMs) are observed in many facets of the immune response. The proline-rich regions are known to preferentially adopt a polyproline type II helical conformation, an extended structure that facilitates transient intermolecular interactions such as signal transduction, antigen recognition, cell-cell communication and cytoskeletal organization. The propensity of both the side chain and the backbone carbonyls of the
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Vlasov, P. K., A. V. Budzko, M. A. Rubin, V. G. Tumanyan, A. A. Makarov, and N. G. Esipova. "Left-handed helix of polyproline ii type in linker regions of DNA-binding proteins." Biophysics 53, no. 6 (2008): 663–64. http://dx.doi.org/10.1134/s0006350908060353.

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Mazuryk, Jarosław, Izabela Puchalska, Kamil Koziński, et al. "PTD4 Peptide Increases Neural Viability in an In Vitro Model of Acute Ischemic Stroke." International Journal of Molecular Sciences 22, no. 11 (2021): 6086. http://dx.doi.org/10.3390/ijms22116086.

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Ischemic stroke is a disturbance in cerebral blood flow caused by brain tissue ischemia and hypoxia. We optimized a multifactorial in vitro model of acute ischemic stroke using rat primary neural cultures. This model was exploited to investigate the pro-viable activity of cell-penetrating peptides: arginine-rich Tat(49–57)-NH2 (R49KKRRQRRR57-amide) and its less basic analogue, PTD4 (Y47ARAAARQARA57-amide). Our model included glucose deprivation, oxidative stress, lactic acidosis, and excitotoxicity. Neurotoxicity of these peptides was excluded below a concentration of 50 μm, and PTD4-induced p
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Dissertations / Theses on the topic "Hélice polyproline de type II"

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Coursindel, Thibault. "Conception, synthèse et valorisation de spirolactames originaux mimant une hélice de type polyproline II." Thesis, Montpellier 2, 2010. http://www.theses.fr/2010MON20063/document.

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Ces travaux de thèse s'inscrivent dans un projet à long terme visant à développer de nouveaux outils nécessaires à l'élucidation de mécanismes biologiques impliquant des interactions de type protéine-protéine mettant en jeu des structures secondaires protéiques de type polyproline II (PPII). En particulier, nous nous sommes intéressés à la conception, synthèse et valorisation de spirolactames originaux capables de mimer une hélice PPII, point de départ dans la recherche de nouvelles molécules d'intérêts thérapeutiques. Cette structure secondaire unique, caractéristique des ligands SH3, joue un
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Cayrou, Chloé. "Conception, Synthèse et Analyse Structurale de Foldamères Fluorés de Conformation Hélicoïdale Polyproline de type II Ciblant des Membranes ou des Protéines Amyloïdes." Electronic Thesis or Diss., CY Cergy Paris Université, 2024. http://www.theses.fr/2024CYUN1308.

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Le terme foldamère désigne tout oligomère capable de se replier en une structure conformationnellement stable en solution. Parmi eux, les foldamères peptidiques semblent particulièrement intéressants pour répondre à plusieurs défis rencontrés avec les peptides en chimie médicinale, tels que leur trop grande flexibilité et leur faible stabilité in vivo. Le caractère structuré des foldamères peut ainsi s’avérer être un atout dans le développement de nouveaux peptides d’intérêt biologique interagissant avec des protéines ou des membranes (Peptides de Pénétration Cellulaire, CPPs ou Peptides AntiM
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Martin, Charlotte. "De la silaproline à la synthèse d'homopolypeptides mimes d'hélice polyproline de type II." Thesis, Montpellier 2, 2013. http://www.theses.fr/2013MON20246/document.

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Les acides α-aminés non naturels forment une famille de composés incontournables pour la conception de peptidomimétiques. Plus précisément, l'utilisation du silicium comme isostère du carbone sur la chaîne latérale des acides α-aminés a été largement reportée dans la littérature, montrant alors l'importance d'une telle modification. En particulier, compte tenu du rôle fondamental que joue la proline dans la structuration des peptides, et des avantages que peut apporter le silicium, il nous a paru intéressant de nous centrer sur la silaproline. Après avoir mis au point une synthèse permettant l
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Chaubet, Guilhem. "Nouvelles réactions de contraction de cycle : outils pour la construction d'édifices organisés." Phd thesis, Université Montpellier II - Sciences et Techniques du Languedoc, 2013. http://tel.archives-ouvertes.fr/tel-01066789.

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Ces travaux de thèse s'inscrivent dans un projet à long terme concernant le développement de nouvelles réactions de contraction de cycle originales afin d'accéder à des édifices moléculaires organisés à activités biologiques potentielles. Généralement découvertes de manière fortuite, les réactions de contraction de cycle sont des réarrangements offrant l'avantage de modifier rapidement le squelette des molécules et permettant donc un accès facile à des analogues structurels, une propriété intéressante et utile aussi bien en chimie de synthèse qu'en chimie médicinale. Dans cette optique, trois
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Book chapters on the topic "Hélice polyproline de type II"

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Siermala, Markku, Martti Juhola, and Mauno Vihinen. "Binary Vector or Real Value Coding for Secondary Structure Prediction? A Case Study of Polyproline Type II Prediction." In Medical Data Analysis. Springer Berlin Heidelberg, 2001. http://dx.doi.org/10.1007/3-540-45497-7_40.

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Siermala Markku, Juhola Martti, and Vihinen Mauno. "Neural Network Prediction of Polyproline Type II Secondary Structures." In Studies in Health Technology and Informatics. IOS Press, 2000. https://doi.org/10.3233/978-1-60750-921-9-475.

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This study considers detection of polyproline type II secondary structures from protein sequences. This difficult problem was handled with multilayer perceptron neural networks, which were found to be useful for such bioinformatics studies. Polyproline II secondary structures have not previously been tried to be predicted from sequences.
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Pazderková Markéta, Kočišová Eva, Pazderka Tomáš, et al. "Antimicrobial peptide from the eusocial bee Halictus sexcinctus interacting with model membranes." In Advances in Biomedical Spectroscopy. IOS Press, 2013. https://doi.org/10.3233/978-1-61499-184-7-079.

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Halictine-1 (Hal-1) – a linear antibacterial dodecapeptide isolated from the venom of the eusocial bee Halictus sexcinctus – has been subjected to a detailed spectroscopic study including circular dichroism, fluorescence and vibrational spectroscopy. We investigated Hal-1's ability to adopt an amphipathic α-helical structure upon interaction with model lipid based bacterial membranes (phosphatidylcholine/phosphatidylglycerol based large unilamellar vesicles, sodium dodecylsulfate micelles) and helix inducing components (trifluoroethanol). It was found that Hal-1 r
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