Добірка наукової літератури з теми "Collagen triple helix"
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Статті в журналах з теми "Collagen triple helix"
Brodsky, Barbara, and John A. M. Ramshaw. "The collagen triple-helix structure." Matrix Biology 15, no. 8-9 (March 1997): 545–54. http://dx.doi.org/10.1016/s0945-053x(97)90030-5.
Повний текст джерелаNewberry, Robert W., Brett VanVeller, and Ronald T. Raines. "Thioamides in the collagen triple helix." Chemical Communications 51, no. 47 (2015): 9624–27. http://dx.doi.org/10.1039/c5cc02685g.
Повний текст джерелаSato, Daisuke, Hitomi Goto, Yui Ishizaki, Tetsuya Narimatsu, and Tamaki Kato. "Design, Synthesis, and Photo-Responsive Properties of a Collagen Model Peptide Bearing an Azobenzene." Organics 3, no. 4 (October 11, 2022): 415–29. http://dx.doi.org/10.3390/org3040027.
Повний текст джерелаFujii, Kazunori K., Yuki Taga, Yusuke K. Takagi, Ryo Masuda, Shunji Hattori, and Takaki Koide. "The Thermal Stability of the Collagen Triple Helix Is Tuned According to the Environmental Temperature." International Journal of Molecular Sciences 23, no. 4 (February 12, 2022): 2040. http://dx.doi.org/10.3390/ijms23042040.
Повний текст джерелаBoryskina, O. P., T. V. Bolbukh, M. A. Semenov, and V. Ya Maleev. "Physical factors of collagen triple helix stability." Biopolymers and Cell 22, no. 6 (November 20, 2006): 458–67. http://dx.doi.org/10.7124/bc.00074d.
Повний текст джерелаHorng, Jia-Cherng, Andrew J. Hawk, Qian Zhao, Eric S. Benedict, Steven D. Burke, and Ronald T. Raines. "Macrocyclic Scaffold for the Collagen Triple Helix." Organic Letters 8, no. 21 (October 2006): 4735–38. http://dx.doi.org/10.1021/ol061771w.
Повний текст джерелаNagai, Naoko, Masanori Hosokawa, Shigeyoshi Itohara, Eijiro Adachi, Takatoshi Matsushita, Nobuko Hosokawa, and Kazuhiro Nagata. "Embryonic Lethality of Molecular Chaperone Hsp47 Knockout Mice Is Associated with Defects in Collagen Biosynthesis." Journal of Cell Biology 150, no. 6 (September 18, 2000): 1499–506. http://dx.doi.org/10.1083/jcb.150.6.1499.
Повний текст джерелаClark, C. C., and C. F. Richards. "Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices." Biochemical Journal 250, no. 1 (February 15, 1988): 65–70. http://dx.doi.org/10.1042/bj2500065.
Повний текст джерелаKAFIENAH, Wa'el, Dieter BRÖMME, David J. BUTTLE, Lisa J. CROUCHER, and Anthony P. HOLLANDER. "Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix." Biochemical Journal 331, no. 3 (May 1, 1998): 727–32. http://dx.doi.org/10.1042/bj3310727.
Повний текст джерелаHe, Xiaofeng, Liling Xie, Xiaoshan Zhang, Fan Lin, Xiaobo Wen, and Bo Teng. "The Structural Characteristics of Collagen in Swim Bladders with 25-Year Sequence Aging: The Impact of Age." Applied Sciences 11, no. 10 (May 17, 2021): 4578. http://dx.doi.org/10.3390/app11104578.
Повний текст джерелаДисертації з теми "Collagen triple helix"
鄭隆峰 and Lung-fung Cheng. "Modelling and sequence analysis of the collagen triple helix." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2001. http://hub.hku.hk/bib/B31969914.
Повний текст джерелаCheng, Lung-fung. "Modelling and sequence analysis of the collagen triple helix." Hong Kong : University of Hong Kong, 2001. http://sunzi.lib.hku.hk/hkuto/record.jsp?B2373615X.
Повний текст джерелаDai, Nan. "I. Collagen-like polypeptides. II. Helix-turn-helix peptides and turn mimetics." Diss., Virginia Tech, 2008. http://hdl.handle.net/10919/28411.
Повний текст джерелаPh. D.
Rahgoshay, Keyvan. "Incorporation de prolines et pseudoprolines fluorées dans des chaînes peptidiques, conséquences conformationnelles et applications." Thesis, Cergy-Pontoise, 2019. http://www.theses.fr/2019CERG1037.
Повний текст джерелаIn this thesis, we approach the synthesis of fluorinated analogs of collagen model peptides (CMP) and the study of their thermodynamic, kinetic and structural characteristics. Our laboratory recently developed the synthesis of fluorinated amino acids analogs of the proline residue (pseudoprolines). Firstly, a preliminary study was carried out on model triplets in order to confirm our fluorinated analogs’ ability to stabilize the pre-requisite conformations of collagen’s triple helix. Once these structural characteristics confirmed, we developed synthetic routes for the incorporation of these fluorinated pseudoprolines in solid phase peptide synthesis (SPPS). Several CMPs (21 residues) incorporating our fluorinated pseudoproline analogs were synthesized. The thermodynamic, kinetic and structural characteristics of these fluorinated CMPs were determined by circular dichroism and NMR. The fluorinated pseudoprolines possess singular properties which enable to acquire detailed insights on their structural surroundings. Thus, they can be considered as 1H and 19F NMR probes. The results obtained in this study also open the way to novel approaches for the synthesis of collagen model peptides
Ip, Wency Wan Sze. "Collagen triple helix repeat containing 1 increases melanoma cell migration, adhesion and survival through modulation of the actin cytoskeleton." Thesis, University of British Columbia, 2009. http://hdl.handle.net/2429/8929.
Повний текст джерелаLalande, Mathieu. "Processus induits par l'irradiation de modèles peptidiques de la triple hélice du collagène en phase gazeuse." Thesis, Normandie, 2018. http://www.theses.fr/2018NORMC235/document.
Повний текст джерелаCollagen is the most abundant protein in mammals, and the main constituent of the extracellular matrix of cartilage. The mechanical properties of this tissue are due to the particular triple helical structure of collagen. In this thesis, we focused on peptidic models of the collagen triple helix in thegas phase, which allows reaching their intrinsic properties, including fundamental processes induced by ionizing radiations. An ion mobility spectrometry study of these systems proved that they retain their structural and stability properties in the absence of solvent. In addition, these stability properties also play a role after irradiation with ionizing photons in an ion trap. Furthermore, we have observed, thanks to mass spectrometry, a transition between photo-excitation and photoionization as the energy of the absorbed photon increases in the VUV-X range. Part of this energy is also redistributed in the vibration modes of the system, increases with photon energy, and induces intramolecular as well as intramolecular fragmentation of the triple helix. For the first time, we irradiated peptides in the gas phase by a carbon ion beam having a kinetic energy relevant in the context of hadrontherapy. A process that was absent from studies with photons has been observed : proton detachment. In the last chapter, the validation of a new experimental device dedicated to the irradiation of proteins and DNA strands in a cross-beam configuration, as well as the first results obtained, will be reported
Chen, Chia-Ching, та 陳佳青. "Study of Cation-π interactions in the stability and self-assembly of collagen triple helix". Thesis, 2010. http://ndltd.ncl.edu.tw/handle/50835071376218003030.
Повний текст джерелаElfert, Susanne Claudia [Verfasser]. "Correlation between triple helix stability of collagen VII and skin fragility in dystrophic epidermolysis bullosa / vorgelegt von Susanne Claudia Elfert." 2009. http://d-nb.info/993806457/34.
Повний текст джерелаJenkins, Cara Lee. "Insights into the determinants of collagen triple helix stability : II. inhibition of RNase A by analogs of 3-prime-uridinemonophosphate /." 2004. http://www.library.wisc.edu/databases/connect/dissertations.html.
Повний текст джерелаWang, Wei-Ming, та 王偉銘. "Effect of Arginine Side Chain Length on β-Hairpin Stability and Effect of the Number of POG Triplets on Heterotrimeric Collagen Triple Helix Stability and Specificity". Thesis, 2017. http://ndltd.ncl.edu.tw/handle/jrs34r.
Повний текст джерела國立臺灣大學
化學研究所
105
Electrostatics is important for protein structure stability. Charged amino acids contribute to these electrostatic interactions. β-Sheet is one of the protein secondary structures and is involved in various protein mis-folding diseases. Different amino acids have different propensities for β-sheet formation. Therefore, it is important to study the propensity of charged amino acids for β-sheet formation. This research focuses on the propensity of arginine (Arg) and arginine analogs with longer and shorter side chains (Agh, Agb, and Agp), and the position dependence of the corresponding sheet propensity. β-Hairpins are the simplest β-sheet structure. Hairpin peptides with arginine and arginine analogs incorporated at different guest sites were synthesized by Fmoc-based solid phase peptide synthesis. Collagen triple helix consists of three polyproline II helices. In this project, different numbers of POG triplets were inserted in the middle of all three heterotrimeric collagen triple helix forming peptides. Thermal denaturation experiments were used to determine the melting temperatures of the collagen triple helices. Thermal equilibration was found to be extremely long at temperatures around the melting transition, and up to 2000 minutes were required for reversible denaturation and renaturation. The melting temperatures were derived by fitting with the thermal denaturation curve, assuming a two-state trimer to monomer equilibrium. The POG triplet was found to stabilize the polyproline II structure in a collagen triple helix. Specificity was gradually decreased with the addition of more POG triplets. This study provides insights into how to use POG triplets to tune the stability and specificity of a collagen triple helix.
Частини книг з теми "Collagen triple helix"
Engel, Jürgen, and Hans Peter Bächinger. "Structure, Stability and Folding of the Collagen Triple Helix." In Topics in Current Chemistry, 7–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/b103818.
Повний текст джерелаChow, Wing Ying. "Investigation of Triple-Helix Collagen Hydroxylation by Solid-State NMR Spectroscopy." In Methods in Molecular Biology, 57–77. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9095-5_5.
Повний текст джерелаShoulders, Matthew D., and Ronald T. Raines. "Modulating Collagen Triple-Helix Stability with 4-Chloro, 4-Fluoro, and 4-Methylprolines." In Advances in Experimental Medicine and Biology, 251–52. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_115.
Повний текст джерелаKusebauch, Ulrike, Lisa Lorenz, Sergio A. Cadamuro, Hans-Jürgen Musiol, Martin O. Lenz, Christian Renner, Josef Wachtveitl, and Luis Moroder. "Light-Switchable Folding/Unfolding of the Collagen Triple Helix with Azobenzene-Containing Model Peptides." In Advances in Experimental Medicine and Biology, 57–59. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-73657-0_25.
Повний текст джерелаRump, Erik T., Dirk T. S. Rijkers, Philip G. de Groot, and Rob M. J. Liskamp. "Stabilization of the Triple Helix of Collagen Peptides Using Fluoroproline and/or Triacid Scaffolds." In Peptides: The Wave of the Future, 379–80. Dordrecht: Springer Netherlands, 2001. http://dx.doi.org/10.1007/978-94-010-0464-0_175.
Повний текст джерелаKaur, Prerna, Hanying Bai, and Hiroshi Matsui. "Genetically Modified Collagen-like Triple Helix Peptide as Biomimetic Template THIS CHAPTER HAS BEEN RETRACTED." In Hybrid Nanomaterials, 251–68. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118003497.ch9.
Повний текст джерелаXu, Yujia. "Thermal Stability of Collagen Triple Helix." In Methods in Enzymology, 211–32. Elsevier, 2009. http://dx.doi.org/10.1016/s0076-6879(09)66009-2.
Повний текст джерелаBrodsky, Barbara, and Anton V. Persikov. "Molecular Structure of the Collagen Triple Helix." In Fibrous Proteins: Coiled-Coils, Collagen and Elastomers, 301–39. Elsevier, 2005. http://dx.doi.org/10.1016/s0065-3233(05)70009-7.
Повний текст джерелаGREEN, RACHEL KRAMER, and HELEN M. BERMAN. "AN OVERVIEW OF STRUCTURAL STUDIES OF THE COLLAGEN TRIPLE HELIX." In Biomolecular Forms and Functions, 17–37. WORLD SCIENTIFIC / INDIAN INST OF SCIENCE, INDIA, 2013. http://dx.doi.org/10.1142/9789814449144_0002.
Повний текст джерелаТези доповідей конференцій з теми "Collagen triple helix"
Deniset-Besseau, A., P. De Sa Peixoto, J. Duboisset, C. Loison, F. Hache, E. Benichou, P. F. Brevet, G. Mosser, and M. C. Schanne-Klein. "Nonlinear optical response of the collagen triple helix and second harmonic microscopy of collagen liquid crystals." In BiOS, edited by Ammasi Periasamy, Peter T. C. So, and Karsten König. SPIE, 2010. http://dx.doi.org/10.1117/12.840873.
Повний текст джерелаRawal, Atul, Kristen L. Rhinehardt, and Ram V. Mohan. "Mechanical Behavior of Collagen Mimetic Peptides Under Fraying Deformation via Molecular Dynamics." In ASME 2019 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/imece2019-11492.
Повний текст джерелаWyatt, Karla E. K., Jonathan W. Bourne, and Peter A. Torzilli. "Deformation-Dependent Enzyme Cleavage of Collagen." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176502.
Повний текст джерелаDeniset-Besseau, A., J. Duboisset, C. Loison, F. Hache, E. Benichou, P. F. Brevet, and M. C. Schanne-Klein. "Second order hyperpolarizability of the collagen triple helix: Measurement and determination of its physical origin." In 11th European Quantum Electronics Conference (CLEO/EQEC). IEEE, 2009. http://dx.doi.org/10.1109/cleoe-eqec.2009.5194760.
Повний текст джерелаZareian, Ramin, Kelli P. Church, and Jeffrey W. Ruberti. "Influence of Mechanical Load on the Degradation of Corneal Collagen." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-193036.
Повний текст джерелаSwickrath, Michael J., Kevin Dorfman, Yoav Segal, and Victor H. Barocas. "The Effect of Composition and Inter- and Intrafibrillar Interactions on the Structure of Collagen IV Networks in the Computer-Simulated Glomerular Basement Membrane." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-205518.
Повний текст джерелаRahgoshay, Keyvan, Anas Terrien, Nathalie Lensen, Thierry Brigaud, Emeric Miclet, and Grégory Chaume. "Use of Trifluoromethylated Pseudoprolines for the Design of Collagen Triple Helix containing Unusual C(5)-Substituted Proline Surrogates." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.206.
Повний текст джерелаCezo, James D., Nicholas Anderson, Eric Kramer, Kenneth D. Taylor, Mark E. Rentschler, and Virginia L. Ferguson. "Tissue Hydration Influences Bursting Pressure of Fused Arteries." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14724.
Повний текст джерелаSun-Hee, Leem, Kang Tae-Hong, Chung Jin Woong, Hwang Yeonsil, Kim Seokho, and Koh Sang Seok. "Abstract A85: Collagen triple helix repeat containing-1 enhances the aggressiveness of pancreatic tumor by increased cancer cell motility and adhesiveness." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-a85.
Повний текст джерелаDeniset-Besseau, A., M. Strupler, J. Duboisset, P. De Sa Peixoto, E. Benichou, C. Fligny, P. L. Tharaux, G. Mosser, P. F. Brevet, and M. C. Schanne-Klein. "Measurement of the quadratic hyperpolarizability of the collagen triple helix and application to second harmonic imaging of natural and biomimetic collagenous tissues." In SPIE Europe Security + Defence, edited by James G. Grote, François Kajzar, and Roberto Zamboni. SPIE, 2009. http://dx.doi.org/10.1117/12.829882.
Повний текст джерела