Relevant bibliographies by topics / Collagen triple helix

Academic literature on the topic 'Collagen triple helix'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Collagen triple helix"

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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.

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Newberry, 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.

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Sato, 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.

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Collagen is a vital component of the extracellular matrix in animals. Collagen forms a characteristic triple helical structure and plays a key role in supporting connective tissues and cell adhesion. The ability to control the collagen triple helix structure is useful for medical and conformational studies because the physicochemical properties of the collagen rely on its conformation. Although some photo-controllable collagen model peptides (CMPs) have been reported, satisfactory photo-control has not yet been achieved. To achieve this objective, detailed investigation of the isomerization behavior of the azobenzene moiety in CMPs is required. Herein, two CMPs were attached via an azobenzene linker to control collagen triple helix formation by light irradiation. Azo-(PPG)10 with two (Pro-Pro-Gly)10 CMPs linked via a photo-responsive azobenzene moiety was designed and synthesized. Conformational changes were evaluated by circular dichroism and the cis-to-trans isomerization rate calculated from the absorption of the azobenzene moiety indicated that the collagen triple helix structure was partially disrupted by isomerization of the internal azobenzene.
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Fujii, 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.

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Triple helix formation of procollagen occurs in the endoplasmic reticulum (ER) where the single-stranded α-chains of procollagen undergo extensive post-translational modifications. The modifications include prolyl 4- and 3-hydroxylations, lysyl hydroxylation, and following glycosylations. The modifications, especially prolyl 4-hydroxylation, enhance the thermal stability of the procollagen triple helix. Procollagen molecules are transported to the Golgi and secreted from the cell, after the triple helix is formed in the ER. In this study, we investigated the relationship between the thermal stability of the collagen triple helix and environmental temperature. We analyzed the number of collagen post-translational modifications and thermal melting temperature and α-chain composition of secreted type I collagen in zebrafish embryonic fibroblasts (ZF4) cultured at various temperatures (18, 23, 28, and 33 °C). The results revealed that thermal stability and other properties of collagen were almost constant when ZF4 cells were cultured below 28 °C. By contrast, at a higher temperature (33 °C), an increase in the number of post-translational modifications and a change in α-chain composition of type I collagen were observed; hence, the collagen acquired higher thermal stability. The results indicate that the thermal stability of collagen could be autonomously tuned according to the environmental temperature in poikilotherms.
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Boryskina, 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.

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Horng, 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.

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Nagai, 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.

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Triple helix formation of procollagen after the assembly of three α-chains at the C-propeptide is a prerequisite for refined structures such as fibers and meshworks. Hsp47 is an ER-resident stress inducible glycoprotein that specifically and transiently binds to newly synthesized procollagens. However, the real function of Hsp47 in collagen biosynthesis has not been elucidated in vitro or in vivo. Here, we describe the establishment of Hsp47 knockout mice that are severely deficient in the mature, propeptide-processed form of α1(I) collagen and fibril structures in mesenchymal tissues. The molecular form of type IV collagen was also affected, and basement membranes were discontinuously disrupted in the homozygotes. The homozygous mice did not survive beyond 11.5 days postcoitus (dpc), and displayed abnormally orientated epithelial tissues and ruptured blood vessels. When triple helix formation of type I collagen secreted from cultured cells was monitored by protease digestion, the collagens of Hsp47+/+ and Hsp47+/− cells were resistant, but those of Hsp47−/− cells were sensitive. These results indicate for the first time that type I collagen is unable to form a rigid triple-helical structure without the assistance of molecular chaperone Hsp47, and that mice require Hsp47 for normal development.
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Clark, 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.

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Matrix-free cells from chick-embryo sterna were incubated with various concentrations of 2,2′-bipyridyl, an iron chelator that inhibits prolyl hydroxylase and lysyl hydroxylase. At concentrations in the region of 0.1 mM, significant effects on cartilage collagen hydroxylation and secretion were observed. When the underhydroxylated collagens were subsequently digested with chymotrypsin or chymotrypsin plus trypsin at 4 degrees C for 15 min, the minor cartilage collagen precursors (namely types IX and XI) were extensively degraded; type II procollagen was only partially susceptible and was converted into underhydroxylated collagen. The results demonstrate that there were significant differences in triple-helix stability among cartilage collagens such that the underhydroxylated minor collagen precursors were unable to attain a native structure under conditions where type II procollagen was successful.
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KAFIENAH, 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.

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Cathepsin K (EC 3.4.22.38) is a recently described enzyme that has been shown to cleave type I collagen in its triple helix. The aim of this study was to determine if it also cleaves type II collagen in the triple helix and to identify the helical cleavage site(s) in types I and II collagens. Soluble human and bovine type II collagen, and rat type I collagen, were incubated with cathepsin K before the reaction was stopped with trans-epoxysuccinyl-l-leucylamido-(4-guanidino)butane (E-64). Analysis by SDS/PAGE of the collagen digests showed that optimal activity of cathepsin K against native type II collagen was between pH 5.0 and 5.5 and against denatured collagen between pH 4.0 and 7.0. The enzyme cleaved telopeptides as well as the α1(II) chains, generating multiple fragments in the range 90–120 kDa. The collagenolytic activity was not due to a contaminating metalloenzyme or serine proteinase as it was not inhibited by 1,10-phenanthroline, EDTA or 3,4-dichloroisocoumarin. Western blotting with anti-peptide antibodies to different regions of the α1(II) chain suggested that cathepsin K cleaved native α1(II) chains in the N-terminal region of the helical domain rather than at the well-defined collagenase cleavage site. This was confirmed by N-terminal sequencing of one of the fragments, revealing cleavage at a Gly-Lys bond, 58 residues from the N-terminus of the helical domain. By using a similar approach, cathepsin K was found to cleave native type I collagen close to the N-terminus of its triple helix. These results indicate that cathepsin K could have a role in the turnover of type II collagen, as well as type I collagen.
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He, 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.

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Aged swim bladders from the yellow drum (Protonibea diacanthus) are considered collagen-based functional food with extremely high market value. The structural integrity of collagen may be crucial for its biological functions. In the current study, swim bladders with 25-year-old sequences were collected and found to be basically composed of collagen. Then, thermogravimetry (TG), differential scanning calorimetry (DSC), X-ray diffraction (XRD), and attenuated total reflectance–Fourier transform infrared spectroscopy (ATR–FTIR) were conducted to evaluate the integrity of the peptide chain and triple helix in the collagen. The structures of microfibers and fiber bundles were revealed with atomic force microscopy (AFM), scanning electrical microscopy (SEM), and optical spectroscopy. The collagens in the aged swim bladders were found to have similar thermal properties to those of fresh ones, but the relative content of the triple helixes was found to be negatively correlated with aging. The secondary structure of the remaining triple helix showed highly retained characteristics as in fresh swim bladders, and the microfibrils also showed a similar D-period to that of the fresh one. However, the fiber bundles displayed more compact and thick characteristics after years of storage. These results indicate that despite 25 years of aging, the collagen in the swim bladders was still partially retained with structures.
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Dissertations / Theses on the topic "Collagen triple helix"

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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.

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Cheng, 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.

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Dai, Nan. "I. Collagen-like polypeptides. II. Helix-turn-helix peptides and turn mimetics." Diss., Virginia Tech, 2008. http://hdl.handle.net/10919/28411.

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Collagen is one of the most important and abundant proteins in mammals. It consists of three left-handed PPII helixes coiled along a common axis to form a very compact right-handed super helix. The primary structure is shown to be (Gly-Xaa-Yaa)n repeats with high content of prolyl residues at both Xaa and Yaa positions. Cis-trans isomerization of the prolyl amide bonds is one of the rate-limiting steps during collagen triple helix folding. The conformationally locked alkene isosteres Fmoc-Gly-Ψ[(E)CH=C]-Pro-Hyp(tBu)-OH and Fmoc-Pro-Ψ[(E)CH=C]-Pro-OH were designed and synthesized. The synthesis of the Gly-Pro isostere had no stereo-control, and the two diastereomers of the tripeptide isostere Fmoc-Gly-Ψ[(E)CH=C]-Pro-Hyp(tBu)-OBn were separated by normal phase HPLC. Although the stereoselectivity of the asymmetric reduction was not good for the Pro-Pro isostere, the resulting diastereomers was separable by flash chromatography, and the absolute stereochemistry of the two diastereomers was determined by Mosher's method. The Gly-Pro alkenyl peptides, and their control peptide Ac-(Gly-Pro-Hyp)8-Gly-Gly-Tyr-NH2 were synthesized and purified. All three peptides showed a maximum around 225 nm and a minimum close to 200 nm in the CD spectra, which indicated the formation of PPII helixes. The Tm value of the control peptide was determined to be 50.0 °C. The peptide with Gly-Ψ[(E)CH=C]-L-Pro-Hyp as the guest triplet formed a stable triple helix with a Tm value of 28.3 °C. The peptide with Gly-Ψ[(E)CH=C]-D-Pro-Hyp as the guest triplet showed a linear decrease in the ellipticity with increasing temperature, which indicated that no triple helix was formed. The Pro-Pro alkenyl peptide and its control peptide H-(Pro-Pro-Gly)₁₀-OH were synthesized and purified. The Tm value of control peptide was determined to be 31.6 °C by extrapolation to 0 M TMAO in PBS buffer, which was very close to the measured value of 31.5 °C. The Pro-Pro alkenyl peptide began to show a maximum around 225 nm in the CD spectra when the concentration of TMAO was higher than 2.5 M. After extrapolation to 0 M TMAO, the Tm value was determined to be –22.0 °C. These results indicate that the backbone inter-chain hydrogen bond is one of the major forces in stabilizing the collagen triple helix, while cis-trans isomerization has limited contribution. The intrinsic properties of the amide bond may have huge influence on the stability of the collagen triple helix. The helix-turn-helix motif is an important tertiary structure in DNA-binding proteins. Stepwise modifications of the Antennapedia HTH peptide (27-55) were performed to improve the helicity and stability. The peptide with more side-chain ion-pairs was over 4 times more helical than the native Antp peptide, while the Ala-based peptide was over 9 times more helical than the native peptide. A 12-membered ring, Fmoc-protected HTH-turn mimic was designed and synthesized, and was ready for solid phase peptide synthesis. The solubility of the cyclic peptide was very poor, and the purification of the final product was very difficult. The solubility problem might also affect solid phase peptide synthesis in the future.
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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.

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Cette thèse porte sur la synthèse d’analogues fluorés de mimes de collagène synthétique et sur l’étude de leurs caractéristiques thermodynamiques, cinétiques et structurales. Notre laboratoire a récemment mis au point la synthèse d'acides aminés fluorés mimes de la proline (pseudoprolines). Dans un premier temps, une étude préliminaire a été effectuée sur des triplets monomériques modèles afin de confirmer l'aptitude de nos mimes fluorés à stabiliser les conformations pré-requises pour la structuration en triple hélice du collagène. Une fois celles-ci confirmées, nous avons ensuite mis au point des voies de synthèse permettant l'incorporation de ces pseudoprolines fluorées en synthèse peptidique sur phase solide. La synthèse de mime de collagène synthétique (21 résidus) incorporant nos analogues fluorés de proline a ensuite été réalisée. Les caractéristiques thermodynamiques, cinétiques et structurales de ces peptides mimes de collagène fluoré ont été déterminées par dichroïsme circulaire et par RMN. Ces pseudoprolines fluorées possèdent des propriétés singulières permettant l’obtention d’informations structurales au niveau local et peuvent ainsi être considérées comme de réelles sondes RMN 1H et 19F. Les résultats obtenus ouvrent également la voie à de nouvelles approches pour la synthèse de mimes peptidiques de collagène
In 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
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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.

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Background: Collagen Triple Helix Repeat Containing 1 (CTHRC1) is a recently discovered extracellular protein that can bind and activate Wnt signaling pathway. In previous gene expression profiling experiments, it was found to be aberrantly upregulated in metastatic melanoma and its expression level was correlated with melanoma progression and metastasis. Objective: The purpose of this study is to understand the functional impact of CTHRC1 on cancer using melanoma cell lines as a model. Experimental Methods: We transfected two melanoma cell lines, MMAN and MMRU, with plasmid vectors to create stable clones with high and low CTHRC1 expression to study the functional effects of CTHRC1 in vitro. Using these two cell lines, we assayed for melanoma migration, adhesion and survival using scratch wound healing assay, attachment assay and cell cycle analysis, respectively. In addition, the cells were stained for F-actin with AlexaFluor 594 labeled phalloidin to observe for actin organization. Results: Using these two pairs of cell lines, we have found that CTHRC1 expression increased melanoma cell migration, enhanced melanoma cell adhesion to both tissue culture plastic and matrigel, and protected melanoma cells from serum deprivation induced apoptosis. Further, it was demonstrated that CTHRC1’s pro-survival effect was dependent on cell adhesion, as the protection effect was lost when melanoma cells were cultured in suspension. Immunofluorescent staining of F-actin revealed that CTHRC1 expression increased the formation structures such as focal complexes, lamellipodia and filopodia. Discussion: The increased formation of the adhesion structures may be the key to CTHRC1 associated cell migration, adhesion and survival. These structures are likely regulated by the Rho family of proteins that act downstream of the Wnt/PCP pathway, with which CTHRC1 has been previously demonstrated to be involved as a co-receptor. Conclusion: Results from this study suggest that CTHRC1 expression promotes cellular behaviours associated with tumour metastases. Therefore, inhibition of this protein may be able to block melanoma metastasis and may have value as a potential therapeutic.
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Lalande, 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.

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Le collagène est la protéine la plus abondante dans les mammifères, et le constituant principal de la matrice extracellulaire du cartilage. Les propriétés mécaniques de ce tissu sont dues à la structure particulière du collagène : la triple hélice. Lors de cette thèse, nous nous sommes intéressés à des peptides modèles de la triple hélice du collagène en phase gazeuse, ce qui permet l’étude de leurs propriétés intrinsèques, dont les processus fondamentaux induits par des rayonnements ionisants. Une étude structurale de ces systèmes par spectrométrie de mobilité ionique a permis de s’assurer qu’ils conservent bien leurs propriétés structurales et de stabilité en l’absence de solvant. De plus, cette stabilité se manifeste aussi lors de l’irradiation par photons ionisants dans un piège à ions. Par ailleurs, nous avons observé, grâce à la spectrométrie de masse, une transition entre photo-excitation et photo-ionisation lorsque l’énergie du photon absorbé augmente dans la gamme VUV-X. Une partie de cette énergie est également redistribuée dans les modes de vibration du système, croît avec l’énergie du photon, et induit la fragmentation inter puis intramoléculaire de la triple hélice. Nous avons également irradié pour la première fois des peptides en phase gazeuse par un faisceau d’ions carbones à l’énergie cinétique pertinente dans le contexte de l’hadronthérapie. Un processus non-observé avec les photons a été mis en évidence : le détachement de proton. Enfin, la validation d’un nouveau dispositif expérimental dédié à l’irradiation de protéines et brins d’ADN par des ions en faisceaux croisés, ainsi que les premiers résultats obtenus, seront abordés
Collagen 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
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Chen, Chia-Ching, and 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.

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Elfert, 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.

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Jenkins, 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.

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Wang, Wei-Ming, and 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.

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碩士
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.
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Book chapters on the topic "Collagen triple helix"

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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.

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Chow, 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.

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Shoulders, 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.

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Kusebauch, 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.

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Rump, 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.

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Kaur, 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.

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Xu, 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.

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Brodsky, 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.

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GREEN, 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.

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Conference papers on the topic "Collagen triple helix"

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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.

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Rawal, 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.

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Abstract Collagen is a pervasive, triple helical, extracellular matrix (ECM) protein, found in human body from skin and bones to blood vessels and lungs, making it biocompatible, biodegradable, capable of cell attachment, and relevant for applications in bio-polymers, tissue engineering and a plethora of other bio-medical fields. Natural collagen’s extraction from natural sources is time consuming, sometimes costly, and it is difficult to render, and could present undesired biological and pathogenic changes. Nanoscale collagen mimetic peptides (Synthetic Collagen), without the unwanted biological entities present in the medium, has shown to mimic the unique properties that are present in natural collagen. Synthetic collagen, thus provides a superior alternative compared to natural collagen for its utilization in several applications. Their properties are affected by surrounding environments, including various solvents, and can be tailored toward specific applications. The focus of this paper is to investigate the mechanical properties of these nanoscale collagen mimetic peptides with lengths of about 10nm, leading to understanding of their feasibility in bio-printing of a composite polymeric collagen biomaterial with a blend of multiple synthetic collagen molecules. Molecular dynamics modeling is used to simulate, model and analyze mechanical properties of synthetic collagen peptides. In particular, mechanical behavior of these peptides are studied. An in-depth insight into the deformation and structural properties of the collagen peptides are of innovative significance for a multitude of bio medical engineering applications. Present paper employed steered molecular dynamics as the principal method of investigating the mechanical properties of nanoscale collagen mimetic peptide 1BKV, which closely resembles natural collagen with a shorter sequence length of 30 amino acids. A detailed comprehension of the protein’s mechanical properties is investigated through fraying deformation behavior studied. A calculated Gibbs free energy value of 40 Kcal/mol corresponds with a complete unfolding of a single alpha-helix peptide chain from a triple helical protein in case of fraying. Force needed for complete separation of the alpha-helix from the triple-helical protein is analyzed, and discussed in this paper.
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Wyatt, 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.

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Collagen degradation is a mechanism for normal musculoskeletal development and extracellular matrix (ECM) maintenance, and in response to trauma, disease and inflammation. Matrix metalloproteinases (MMP-1, 8, and 13, the collagenases) are the primary enzymes that act to degrade collagen. These MMPs gain access to the collagen triple helix by binding to the enzyme’s attachment domain along the α-chains, followed by separation (unwinding) of the α-chains to expose the 3/4–1/4 cleavage site, and then cleavage of the α-chain by the enzyme’s catalytic domain [3, 5].
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Deniset-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.

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Zareian, 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.

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Collagen is one of the most important structural proteins in vertebrate animals. Over 25 different types of collagen have been identified, but type I collagen is the most abundant fibril forming collagen and contributes to the structural performance numerous connective tissues including ligaments, tendons and cornea [1]. In addition to collagen self-assembly, collagen degradation is an important step in the development, remodeling, homeostasis and pathology of load-bearing ECM. Matrix Metalloproteinase (MMP) types I and VIII, bacterial collagenase and cathepsin are the best known enzymes capable of directly degrading the collagen triple helix [2, 3]. Several researchers have hypothesized that straining collagen fibrils makes them less susceptible to enzymatic degradation [4, 5]. This concept, which we refer to as “strain-stabilization” has important implications for our understanding of collagen as an engineering material.
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Swickrath, 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.

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The glomerular basement membrane of the kidney, responsible for performing ultrafiltration blood plasma, is largely comprised of type-IV collagen and laminin. Type-IV collagen self-assembles into a heterotrimer composed of three distinct domains (fig. 1A): (1) the globular non-collagenous NCl domain of ∼10 nm in diameter, (2) the non-collagenous 7S domain ∼30 nm in length and ∼3nm in diameter, and (3) the collagenous triple helix of ∼370 nm in length and ∼3 nm in diameter composed of a repeating Gly-X-Y subunit [1]. The heterotrimers associate with remarkable specificity from six genetically distinct α-chains, α1(IV) to α6(IV) forming α1α1α2, α3α4α5, and α5α5α6 heterotrimers [2]. In the healthy glomerulus, α1α1α2 ([α1]2α2) is the predominate collagen while significant α3α4α5 is present; α5α5α6 exists only in negligible quantities [2].
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Rahgoshay, 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.

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Cezo, 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.

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Tissue fusion is a complex thermally driven reaction which, through the application of heat and pressure, bonds the extracellular matrix (ECM) of neighboring tissues together. While the mechanism of this reaction is unknown, several theories do exist. Collagen is largely thought to be responsible for the formation of the fusion bond [1–3]. During tissue fusion, as the tissue temperature is elevated (> 100 °C) [4–5], collagen denatures and water is forcibly evaporated out of the tissue [6–11]. Collagen in arterial tissue is comprised of a tightly wound triple helix held in place by crosslinking. Upon denaturation, the crosslinks are broken and the helix unwinds [6–8]. It is theorized that under applied heat and pressure the denatured molecules tangling with adjacent molecules [1], crosslinking to neighboring molecules [2], or a combination of these two mechanisms are responsible for the formation of the tissue fusion bond [3]. Water is also present in the ECM which can be classified as free or bound. Free water is able to diffuse and move freely around the ECM. Bound water is held to ECM proteins through dipole interactions. During tissue fusion, the water is forcibly removed and these charged sites which interact with water are now able to interact with adjacent molecules. These charged sites would not exist if not for the removal of water from the ECM. The goal of this study is to elucidate the importance of water in the formation of the tissue fusion bond.
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Sun-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.

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Deniset-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.

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