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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 董成淵(Chen-Yuan Dong) | |
| dc.contributor.author | Tsung-Hsien Li | en |
| dc.contributor.author | 李宗憲 | zh_TW |
| dc.date.accessioned | 2021-06-15T00:49:32Z | - |
| dc.date.available | 2008-09-02 | |
| dc.date.copyright | 2008-09-02 | |
| dc.date.issued | 2008 | |
| dc.date.submitted | 2008-08-19 | |
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So, P.T.C., Dong, C.Y., Masters, B.R. & Berland, K.M. Two-photon excitation fluorescence microscopy. Annual Review of Biomedical Engineering 2, 399-429 (2000). 14. Chu, S.W., et al. Studies of x((2))/x((3)) tensors in submicron-scaled bio-tissues by polarization harmonics optical microscopy. Biophysical Journal 86, 3914-3922 (2004). 15. Carmeliet, P. & Jain, R.K. Angiogenesis in cancer and other diseases. Nature 407, 249-257 (2000). 16. Li, F.C., et al. Dorsal skin fold chamber for high resolution multiphoton imaging. Optical and Quantum Electronics 37, 1439-1445 (2005). 17. Stoller, P., Kim, B.M., Rubenchik, A.M., Reiser, K.M. & Da Silva, L.B. Polarization-dependent optical second-harmonic imaging of a rat-tail tendon. Journal of Biomedical Optics 7, 205-214 (2002). 18. Boyd, R.W. Nonlinear Optics, (Academic Press, 2003). 19. Liu, S.H., Yang, R.S., al-Shaikh, R. & Lane, J.M. Collagen in tendon, ligament, and bone healing. A current review. Clin Orthop Relat Res 318, 265-278 (1995). 20. Venturoni, M., Gutsmann, T., Fantner, G.E., Kindt, J.H. & Hansma, P.K. Investigations into the polymorphism of rat tail tendon fibrils using atomic force microscopy. Biochemical and Biophysical Research Communications 303, 508-513 (2003). 21. Engel, J. Biochemistry - Versatile collagens in invertebrates. Science 277, 1785-1786 (1997). 22. Brinckmann, J., Notbohm, H. & Muller, P.K. Collagen: Primer in Structure, Processing and Assembly, (Springer, 2005). 23. Nelson, D.L., Cox, M.M. & Lehninger, A. Lehninger principles of biochemistry, (W. H. Freeman ; Palgrave, New York; Basingstoke, 2004). 24. Keene, D.R., Oxford, J.T. & Morris, N.P. Ultrastructural-Localization of Collagen Type-Ii, Type-Ix, and Type-Xi in the Growth-Plate of Human Rib and Fetal Bovine Epiphyseal Cartilage - Type-Xi Collagen Is Restricted to Thin Fibrils. Journal of Histochemistry & Cytochemistry 43, 967-979 (1995). 25. Fertala, A., Holmes, D.F., Kadler, K.E., Sieron, A.L. & Prockop, D.J. Assembly in Vitro of Thin and Thick Fibrils of Collagen II from Recombinant Procollagen II. THE MONOMERS IN THE TIPS OF THICK FIBRILS HAVE THE OPPOSITE ORIENTATION FROM MONOMERS IN THE GROWING TIPS OF COLLAGEN I FIBRILS. Journal of Biological Chemistry 271, 14864 (1996). 26. Prockop, D.J. & Fertala, A. The Collagen Fibril: The Almost Crystalline Structure. Journal of Structural Biology 122, 111-118 (1998). 27. Fertala, A., Han, W.B. & Ko, F.K. Mapping critical sites in collagen II for rational design of gene-engineered proteins for cell-supporting materials. Journal of Biomedical Materials Research 57, 48-58 (2001). 28. Tsuzaki, M., Yamauchi, M. & Banes, A.J. Tendon Collagens - Extracellular-Matrix Composition in Shear-Stress and Tensile Components of Flexor Tendons. Connective Tissue Research 29, 141-152 (1993). 29. Eyre, D. Collagen of articular cartilage. Arthritis Res 4, 30-35 (2002). 30. Chou, C.K., et al. Polarization ellipticity compensation in polarization second-harmonic generation microscopy without specimen rotation. Journal of Biomedical Optics 13, - (2008). 31. Richards, B. & Wolf, E. Electromagnetic Diffraction in Optical Systems. II. Structure of the Image Field in an Aplanatic System. Proceedings of the Royal Society of London. Series A, Mathematical and Physical Sciences (1934-1990) 253, 358-379 (1959). 32. Markwardt, C.B. MPFITFUN. NASA/GSFC Code 662, Greenbelt, MD 20770 (http://cow.physics.wisc.edu/~craigm/idl/idl.html, 2007). 33. Markwardt, C.B. MPFIT. NASA/GSFC Code 662, Greenbelt, MD 20770 (http://cow.physics.wisc.edu/~craigm/idl/idl.html, 2007). 34. Yeh, A.T., et al. Nonlinear optical microscopy of articular cartilage. Osteoarthritis and Cartilage 13, 345-352 (2005). 35. Lee, H.S., et al. Imaging human bone marrow stem cell morphogenesis in polyglycolic acid scaffold by multiphoton microscopy. Tissue Engineering 12, 2835-2841 (2006). | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/42151 | - |
| dc.description.abstract | 膠原蛋白是人體中非常重要的一種蛋白質，其分子由三條多肽鏈纏繞而成，具有三股螺旋結構。依據多肽鏈中的胺基酸序列的不同，可以將目前已知的膠原蛋白分為29種類型。
光學顯微術中，利用偏振二倍頻顯微術來掃描生物樣品，可以得到其分子尺度上的資訊，但考慮到光學元件，如分光鏡，會改變光的偏振性。因此，我們使用了二分之一波長片及四分之一波長片來彌補這種效應，同時也藉此旋轉雷射的偏振角度。如此一來，我們校正了分光鏡造成的偏振性改變，也減少了轉動樣品所帶來的困擾。 藉由分析隨著入射光的偏振角度而改變的二倍頻強度變化，我們可以分析出生物樣品內膠原蛋白的二階極化率張量，並且推導出膠原蛋白分子的螺旋角。此實驗中，我們使用了大鼠尾巴的肌腱和豬腿骨間的關節軟骨來做比較，他們分別含有大量的第一類及第二類的膠原蛋白，而這兩種不同類型的膠原蛋白分析出來的二階極化率張量及螺旋角確實有所不同！第一類和第二類膠原蛋白分子的螺旋角分別為49.1°±1.3° and 52.8°±2.7°。證明了偏振二倍頻顯微術能夠有效的分辨第一類及第二類的膠原蛋白。 | zh_TW |
| dc.description.abstract | Collagen is one of the most important and abundant protein in human body. Its molecules composed of three entwined polypeptide chains. There are currently 29 known types of collagen differentiated by the sequence of residues in each polypeptide chain.
Utilizing polarized second harmonic generation microscopy, we can obtain structural information at the molecular level. In order to compensate the depolarization effects of optical component such as the dichroic mirror, we used the combination of a half-wave plate and a quarter-wave plate to rotate the polarization angle of the laser incident on the sample. This allows us to perform polarization microscopy without the drawbacks of sample rotation. By measuring second harmonic generation intensity variation as a function of the polarization angle of the incident light, we can analyze the second-order susceptibility tensor of collagen in a biological sample and determinate the pitch angle of the collagen helix. In this study, we compared the second-order susceptibility tensor of collagen from rat tail tendon and cartilage of porcine femoral-tibial joint, which contain abundant type I and type II collagens respectively. We found that the second-order susceptibility tensor and the calculated pitch angle for type I and II collagen to be 49.20°±0.34° and 52.43°±0.72°. Our results suggest that polarized SHG microscopy could potentially be used for distinguishing these two types of collagen. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-15T00:49:32Z (GMT). No. of bitstreams: 1 ntu-97-R95222070-1.pdf: 2445463 bytes, checksum: 64de849539d28081a6dbc3ca2da1dc1b (MD5) Previous issue date: 2008 | en |
| dc.description.tableofcontents | 致謝 II
摘要 III Abstract IV Contents VI Figure Catalog VII Table Catalog VII Chapter 1 Introduction 1 Chapter 2 Basic Principle 4 2.1 Theory of second harmonic generation 4 Basics of second harmonic generation process 4 Intrinsic permutation symmetry of nonlinear susceptibility 6 Effect of inversion symmetry on second-order polarization 7 Kleinman’s symmetry 8 Contracted notation 9 2.2 SHG microscopy 10 Optical resolution 10 Mode-locking laser 13 2.3 Use of wave plates for ellipticity compensation 16 Compensation for the retardation phase due to dichroic 16 Calibration of power variation due to dichroic 21 Chapter 3 Collagen 24 3.1 Overview of collagen 24 Basic information 24 Subfamily 25 Arrangement of collagen 26 3.2 Second order susceptibility of collagen fiber 29 3.3 Collagen in rat-tail tendon and cartilage 31 Chapter 4 Experimental Setup 32 4.1 Configuration of instruments 32 4.2 Sample preparation 34 4.3 Experimental and analytical methods 37 Chapter 5 Results and Discussion 39 Chapter 6 Conclusion 48 References 50 | |
| dc.language.iso | en | |
| dc.subject | 偏振 | zh_TW |
| dc.subject | 膠原蛋白 | zh_TW |
| dc.subject | 二倍頻 | zh_TW |
| dc.subject | 非線性極化率 | zh_TW |
| dc.subject | 螺旋結構 | zh_TW |
| dc.subject | 軟骨 | zh_TW |
| dc.subject | 螺旋角 | zh_TW |
| dc.subject | 肌腱 | zh_TW |
| dc.subject | pitch angle | en |
| dc.subject | second harmonic generation | en |
| dc.subject | collagen | en |
| dc.subject | polarization | en |
| dc.subject | tendon | en |
| dc.subject | cartilage | en |
| dc.subject | nonlinear susceptibility | en |
| dc.subject | helical structure | en |
| dc.title | 利用偏振二倍頻顯微術分析第一類與第二類膠原蛋白的結構 | zh_TW |
| dc.title | Structural Analysis of Type I and Type II Collagen by Polarized Second Harmonic Generation Microscopy | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 96-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 張顏暉(Yuan-Huei Chang),林頌然(Sung-Jan Lin),李宣書(Hsuan-Shu Lee) | |
| dc.subject.keyword | 二倍頻,膠原蛋白,偏振,肌腱,軟骨,非線性極化率,螺旋結構,螺旋角, | zh_TW |
| dc.subject.keyword | second harmonic generation,collagen,polarization,tendon,cartilage,nonlinear susceptibility,helical structure,pitch angle, | en |
| dc.relation.page | 52 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2008-08-19 | |
| dc.contributor.author-college | 理學院 | zh_TW |
| dc.contributor.author-dept | 物理研究所 | zh_TW |
| 顯示於系所單位： | 物理學系 | |
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