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完整後設資料紀錄
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.advisor | 陳平(Richard P. Cheng) | |
dc.contributor.author | Yi-Jen Weng | en |
dc.contributor.author | 翁乙壬 | zh_TW |
dc.date.accessioned | 2021-05-16T16:27:54Z | - |
dc.date.available | 2018-03-06 | |
dc.date.available | 2021-05-16T16:27:54Z | - |
dc.date.copyright | 2013-03-06 | |
dc.date.issued | 2013 | |
dc.date.submitted | 2013-01-23 | |
dc.identifier.citation | Chapter 1
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Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type. Nature 1953, 171, 59-61. 4. Sodek, J.; Hodges, R. S.; Smillie, L. B.; Jurasek, L. Amino-acid sequence of rabbit skeletal tropomyosin and its coiled-coil structure. Proc. Natl. Acad. Sci. U. S. A. 1972, 69, 3800-3804. 5. Wilson, I. A.; Skehel, J. J.; Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 1981, 289, 366-373. 6. Cohen, C.; Parry, D. A. α-helical coiled coils: more facts and better predictions. Science 1994, 263, 488-489. 7. Newman, J.; Keating, A. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science 2003, 300, 2097-2198. 8. Vinson, C.; Myakishev, M.; Acharya, A.; Mir, A.; Moll, J.; Bonovich, M. Classification of human B-ZIP proteins based on dimerization properties. Mol. Cell. Biol. 2002, 22, 6321-6356. 9. Ellenberger, T.; Brandl, C.; Struhl, K.; Harrison, S. 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dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/6388 | - |
dc.description.abstract | 雙螺旋由2到5個α螺旋互相纏繞而成,是個生物體內常見的結構單元。雙螺旋存在於轉錄因子、肌肉收縮系統、細胞骨架等系統之中,而這些生理功能來自於雙螺旋明確且穩定的結構。此研究探討了位在雙螺旋交界面的d位置殘基的側鏈結構對於雙螺旋穩定度的影響。研究所使用的雙螺旋系統為GCN4,將其第二個d位置殘基 (Leu12) 替換成帶有各式結構與極性的胺基酸。IaLd雙螺旋則用來測定胺基酸本身對於雙螺旋結構的偏好程度。實驗利用固相胜肽合成法來合成出各個雙螺旋,藉由圓二色光譜儀來監控由鹽酸胍促成的雙螺旋變性過程,並計算出雙螺旋變性的自由能。除此之外,也利用薄層色層分析法量測了胺基酸的疏水性。至於胺基酸的側鏈結構則以各種結構參數去描述,這些參數包含Es, MR, [L, B1, B5]和側鏈體積。數據分析顯示,當雙螺旋的d位置殘基為烷基時,側鏈結構和胺基酸疏水性兩者相比之下,側鏈結構對於雙螺旋穩定度的影響較大。 | zh_TW |
dc.description.abstract | Coiled coil is a superhelical twist formed by two to five wrapping α-helices. It is a common structural motif that can be found in transcription factors, cytoskeletal systems, contractile systems and etc. These biochemical roles rely on well-defined and stable structures of coiled coils. Accordingly, the effect of side chain structure of d-position residue, which is buried in the coiled coil interface, on coiled coil stability was investigated. GCN4 coiled coil was employed, of which the 2nd d-residue (Leu12) was substituted with various amino acids. IaLd coiled coils were used to obtain the coiled coil propensities of these amino acids. Guanidinium denaturation of the coiled coils was monitored by circular dichroism spectroscopy. Free energy of unfolding was derived from the guanidinium denaturation data. The hydrophobicities of the amino acids were measured by thin layer chromatography. Structural parameters Es, MR, [L, B1, B5], and side chain volume were employed in the analysis. Results show that the shape and size of the residue side chain contribute more than hydrophobicity to the coiled coil stability in coiled coils with the d-position residue bearing aliphatic side chains. | en |
dc.description.provenance | Made available in DSpace on 2021-05-16T16:27:54Z (GMT). No. of bitstreams: 1 ntu-102-R99223123-1.pdf: 24227472 bytes, checksum: ba709cfc66d9b3c3728861b8ce3a4c28 (MD5) Previous issue date: 2013 | en |
dc.description.tableofcontents | 口試委員審定書 (I)
誌謝 (II) 中文摘要 (III) Abstract (IV) Table of Contents (V) List of Figures (VII) List of Tables (IX) Abbreviations (X) Chapter 1 Introduction (1) 1.1 Proteins (2) 1.2 Protein Structures (4) 1.3 Forces in Protein Folding (6) 1.4 α-Helix (8) 1.5 Coiled coil (10) 1.6 Thesis Overview (11) 1.7 References (12) Chapter 2 Effect of Side Chain Structure of d-Position Residue on Coiled Coil Stability (15) 2.1 Introduction (16) 2.1.1 Coiled Coils in Biological Systems (16) 2.1.2 GCN4 Coiled Coil Motif (17) 2.1.3 Coiled Coil Sequence and Structure (18) 2.1.4 Knobs-Into-Holes Interactions of a Dimeric Coiled Coil (21) 2.1.5 Coiled Coil Stability (21) 2.1.6 Chapter Overview (26) 2.2 Results and Discussions (27) 2.2.1 Design of GCN4-Derived Peptides (27) 2.2.2 Peptide Synthesis of GCN4-Derived Peptides (30) 2.2.3 UV-Visible Spectroscopy (UV-vis) of GCN4-Derived Peptides (32) 2.2.4 Circular Dichroism (CD) Spectroscopy of GCN4-Derived Peptides (33) 2.2.5 Guanidinium Denaturation of GCN4-Derived Peptides (37) 2.2.6 ΔGunfold, H2O of GCN4-Derived Peptides (43) 2.2.7 Design of IaLd-Derived Peptides (47) 2.2.8 Peptide Synthesis of IaLd-Derived Peptides (49) 2.2.9 UV-Visible Spectroscopy (UV-vis) of IaLd-Derived Peptides (50) 2.2.10 Circular Dichroism (CD) Spectroscopy of IaLd-Derived Peptides (50) 2.2.11 Guanidinium Denaturation of IaLd-Derived Peptides (53) 2.2.12 ΔGunfold, H2O of IaLd-Derived Peptides (57) 2.2.13 Measuring Hydrophobicities of the Amino Acids (58) 2.2.14 Size and Shape Parameters (59) 2.2.15 Discussion (60) 2.3 Conclusion (65) 2.4 Acknowledgement (65) 2.5 Experimental Section (66) 2.5.1 General Materials and Methods (66) 2.5.2 Peptide Synthesis (70) 2.5.3 UV-Visible Spectroscopy (88) 2.5.4 Circular Dichroism Spectroscopy (88) 2.5.5 Guanidinium Denaturation (89) 2.5.6 Derivation of ΔGunfold, H2O (90) 2.5.7 Measurement of Hydrophobicity by Thin Layer Chromatography (91) 2.5.8 Calculation of Side Chain Volume (91) 2.6 References (92) 2.7 Appendix (97) 2.7.1 Guanidinium Denaturation Curves of GCN4-Xaa (97) 2.7.2 Guanidinium Denaturation Curves of IaLd-Xaa (100) 2.7.3 NMR Spectrum of Fmoc-Allo Ile-OH (102) 2.7.4 NMR Spectrum of Fmoc-Cpa-OH (103) 2.7.5 NMR Spectrum of Fmoc-Nle-OH (104) 2.7.6 ESI-MS Spectrum of Fmoc-Allo Ile-OH (105) 2.7.7 ESI-MS Spectrum of Fmoc-Cpa-OH (106) 2.7.8 ESI-MS Spectrum of Fmoc-Nle-OH (107) 2.7.9 Elsevier License for Reprint of Figure (108) | |
dc.language.iso | en | |
dc.title | d位置胺基酸的側鏈結構對於雙螺旋穩定度的影響 | zh_TW |
dc.title | Effect of Side Chain Structure of d-Position Residue on Coiled Coil Stability | en |
dc.type | Thesis | |
dc.date.schoolyear | 101-1 | |
dc.description.degree | 碩士 | |
dc.contributor.oralexamcommittee | 陳佩燁(Rita P.-Y. Chen),黃人則(Joseph Jen-Tse Huang) | |
dc.subject.keyword | 雙螺旋,GCN4,α螺旋偏好程度,胺基酸疏水性,側鏈結構, | zh_TW |
dc.subject.keyword | coiled coil,GCN4,helix propensity,amino acid hydrophobicity,side chain structure, | en |
dc.relation.page | 108 | |
dc.rights.note | 同意授權(全球公開) | |
dc.date.accepted | 2013-01-23 | |
dc.contributor.author-college | 理學院 | zh_TW |
dc.contributor.author-dept | 化學研究所 | zh_TW |
顯示於系所單位: | 化學系 |
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