Academic literature on the topic 'PolyProline II type helix'

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Journal articles on the topic "PolyProline II type helix"

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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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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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Feng, Chuang, Zhen Wang, Guokun Li, Xiaohan Yang, Nannan Wu, and Lei Wang. "BERT-PPII: The Polyproline Type II Helix Structure Prediction Model Based on BERT and Multichannel CNN." BioMed Research International 2022 (August 24, 2022): 1–14. http://dx.doi.org/10.1155/2022/9015123.

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Predicting the polyproline type II (PPII) helix structure is crucial important in many research areas, such as the protein folding mechanisms, the drug targets, and the protein functions. However, many existing PPII helix prediction algorithms encode the protein sequence information in a single way, which causes the insufficient learning of protein sequence feature information. To improve the protein sequence encoding performance, this paper proposes a BERT-based PPII helix structure prediction algorithm (BERT-PPII), which learns the protein sequence information based on the BERT model. The BE
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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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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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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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Meirson, Tomer, David Bomze, Gal Markel та Abraham O. Samson. "κ-helix and the helical lock and key model: a pivotal way of looking at polyproline II". Bioinformatics 36, № 12 (2020): 3726–32. http://dx.doi.org/10.1093/bioinformatics/btaa186.

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Abstract Motivation Polyproline II (PPII) is a common conformation, comparable to α-helix and β-sheet. PPII, recently termed with a more generic name—κ-helix, adopts a left-handed structure with 3-fold rotational symmetry. Lately, a new type of binding mechanism—the helical lock and key model was introduced in SH3-domain complexes, where the interaction is characterized by a sliding helical pattern. However, whether this binding mechanism is unique only to SH3 domains is unreported. Results Here, we show that the helical binding pattern is a universal feature of the κ-helix conformation, prese
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Schweitzer-Stenner, Reinhard, Bridget Milorey, and Harald Schwalbe. "Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues." Biomolecules 12, no. 5 (2022): 684. http://dx.doi.org/10.3390/biom12050684.

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Flory’s random coil model assumes that conformational fluctuations of amino acid residues in unfolded poly(oligo)peptides and proteins are uncorrelated (isolated pair hypothesis, IPH). This implies that conformational energies, entropies and solvation free energies are all additive. Nearly 25 years ago, analyses of coil libraries cast some doubt on this notion, in that they revealed that aromatic, but also β-branched side chains, could change the 3J(HNHCα) coupling of their neighbors. Since then, multiple bioinformatical, computational and experimental studies have revealed that conformational
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Renugopalakrishnan, V., L. A. Carreira, T. W. Collette, J. C. Dobbs, G. Chandraksasan, and R. C. Lord. "Non-Uniform Triple Helical Structure in Chick Skin Type I Collagen on Thermal Denaturation: Raman Spectroscopic Study." Zeitschrift für Naturforschung C 53, no. 5-6 (1998): 383–88. http://dx.doi.org/10.1515/znc-1998-5-613.

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The individual chains in the triple helix of collagen occur in a conformation related to polyproline II because of the presence of large number of imino peptide bonds. However, these residues are not evenly distributed in the collagen molecule which also contains many non-imino residues. These non-imino regions of collagen may be expected to show preference for other than triple helical conformations. The appearance of several Raman bands in solution phase at 65 °C raises the possibility of non-uniform triple helical structure in collagen. Raman spectroscopic studies on collagen in the solid s
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Pazderková, Markéta, Eva Kočišová, Tomáš Pazderka, et al. "Antimicrobial Peptide from the Eusocial BeeHalictus sexcinctusInteracting with Model Membranes." Spectroscopy: An International Journal 27 (2012): 497–502. http://dx.doi.org/10.1155/2012/840956.

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Halictine-1 (Hal-1)—a linear antibacterial dodecapeptide isolated from the venom of the eusocial beeHalictus sexcinctus—has been subjected to a detailed spectroscopic study including circular dichroism, fluorescence, and vibrational spectroscopy. We investigated Hal-1 ability to adopt an amphipathicα-helical structure upon interaction with model lipid-based bacterial membranes (phosphatidylcholine/phosphatidylglycerol-based large unilamellar vesicles and sodium dodecylsulfate micelles) and helix inducing components (trifluoroethanol). It was found that Hal-1 responds sensitively to the composi
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Dissertations / Theses on the topic "PolyProline II type helix"

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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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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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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 "PolyProline II type helix"

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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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Leydesdorff, Loet. "Towards a Calculus of Redundancy." In Qualitative and Quantitative Analysis of Scientific and Scholarly Communication. Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-59951-5_4.

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AbstractIn this chapter, I extend Shannon’s linear model of communication into a model in which communication is differentiated both vertically and horizontally (Simon, 1973). Following Weaver (1949), three layers are distinguished operating in relation to one another: (i) at level A, the events are sequenced historically along the arrow of time, generating Shannon-type information (that is, uncertainty); (ii) the incursion of meanings at level B is referential to (iii) horizons of meaning spanned by codes in the communication at level C. In other words, relations at level A are first distingu
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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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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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Creamer, Trevor P., and Margaret N. Campbell. "Determinants of the polyproline II helix from modeling studies." In Unfolded Proteins. Elsevier, 2002. http://dx.doi.org/10.1016/s0065-3233(02)62010-8.

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Hornyak, Thomas J., Nancy M. Chung,, and Masayoshi Tachibana. "MITF and the Waardenburg Type II and Albinism–Deafness (Tietz) Syndromes." In Inborn Errors Of Development. Oxford University PressNew York, NY, 2008. http://dx.doi.org/10.1093/oso/9780195306910.003.0114.

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Abstract Microphthalmia-associated transcription factor (MITF) is a member of a large family of proteins with basic helix–loop–helix leucine zipper (bHLHZip) domains. Mutations in this transcription factor initially have been described in mice showing microphthalmia, variable pigmentary loss, and hearing deficit. Similar phenotypes can be seen in humans with Waardenburg Type II Syndrome (WS2) and Albinism–Deafness (Tietz) Syndrome with mutations in MITF. The manifestations of MITF mutations result from loss of melanocytes in the eyes, skin, and cochlea emphasizing the importance of this protei
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Conference papers on the topic "PolyProline II type helix"

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Kahraman, Ahmet. "Dynamic Analysis of a Multi-Mesh Helical Gear Train." In ASME 1992 Design Technical Conferences. American Society of Mechanical Engineers, 1992. http://dx.doi.org/10.1115/detc1992-0046.

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Abstract In this paper, the dynamic behavior of a multi-mesh helical gear train is studied. The gear train consists of three helical gears, with one of the gears in mesh with the other two. An 18-degree-of-freedom dynamic model which includes transverse, torsional, axial and rotational (rocking) motions of the flexibly mounted gears is developed. Two different loading conditions are identified. For case I, the system is driven by the gear in the middle, and for case II, the system is driven by one of the gears at either end of the gear train. Gear mesh phases under each loading condition are d
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Batista, Michael, Hadi T. Nia, Karen Cox, et al. "Effects of Chondroadherin on Cartilage Nanostructure and Biomechanics via Murine Model." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14516.

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While small leucine rich proteins/proteoglycans (SLRPs) are present in very low concentrations in the extracellular matrix (ECM), they have been shown to be critical determinants of the proper ECM assembly and function in connective tissues [1] including bone [2], cornea [3], and cartilage [4]. However, their direct and indirect roles in matrix biomechanics and the potential for osteoarthritis-related dysfunction of cartilage remain unclear. With the advent of new high resolution nanotechnological tools, the direct quantification of cartilage biomechanical properties using murine models can pr
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