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課程名稱 |
分子辨識
Molecular Recognition |
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開課學期 |
109-1 |
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授課對象 |
生命科學院 基因體與系統生物學學位學程 |
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授課教師 |
徐駿森 |
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課號 |
AC5066 |
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課程識別碼 |
623 U4340 |
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班次 |
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學分 |
2.0 |
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全/半年 |
半年 |
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必/選修 |
選修 |
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上課時間 |
星期三8,9(15:30~17:20) |
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上課地點 |
農化一第五 |
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備註 |
總人數上限：20人 |
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Ceiba 課程網頁 |
http://ceiba.ntu.edu.tw/1091AC5066_MR |
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課程簡介影片 |
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核心能力關聯 |
核心能力與課程規劃關聯圖 |
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課程大綱
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課程概述 |
分子辨識課程是應用結構生物、化學生物與分子生物學來探討生命科學的一門課。無論在動物、植物或是微生物的系統，生命現象從微觀的角度來看就是細胞內生物分子經由交互作用而造成訊息傳遞與命令執行之功能。此外，醫學或農業上的病毒或病菌感染、也是藉由特定分子的辨識為起始，進而入侵宿主。瞭解這些生物分子之分子辨識作用，除了能說明其作用機制，並在應用上可發展策略用於抑制或促進其辨識作用及生物活性。 |
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課程目標 |
此課程以深入淺出的方式，一開始說明分子辨識的化學原理，接著介紹各項研究分子交互作用之結構與生物物理工具。並以數個具有啟發性的生物交互作用系統為範例。最後由文獻討論來讓參與課程者能將分子結構觀念帶入本身正在研究或有興趣的領域。 |
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課程要求 |
歡迎大三以上與研究所不同背景學生，但若未修過生物化學，請先與老師溝通。 |
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預期每週課後學習時數 |
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Office Hours |
每週三 13:00~15:00 |
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指定閱讀 |
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參考書目 |
Arthur M. Lesk, (2004). Introduction of Protein Science. Oxford University Press.
Gordon C.K. Roberts, (2000). NMR of Macromolecules-A practical approach, Oxford University Press.
Gale Rhodes, (2000). Crystallography Made Crystal Clear, Academic Press
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評量方式
(僅供參考) |
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No. |
項目 |
百分比 |
說明 |
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1. |
報告 |
30% |
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2. |
作業 |
20% |
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3. |
期末考 |
30% |
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4. |
期中考 |
20% |
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週次 |
日期 |
單元主題 |
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第1週 |
9/16 |
Introduction |
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第2週 |
9/23 |
Structural and Chemical Properties of Biological Macromolecules |
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第3週 |
9/30 |
Protein Crystallography |
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第4週 |
10/7 |
Electron Microscopy |
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第5週 |
10/14 |
Principle of Nuclear Magnetic Resonance Spectroscopy:
(I)Biomolecular NMR technique |
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第6週 |
10/21 |
Principle of Nuclear Magnetic Resonance Spectroscopy:
(II)Multi-dimesional NMR for protein determination |
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第7週 |
10/28 |
Structural Bioinformatics |
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第8週 |
11/4 |
Structural Bioinformatics |
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第9週 |
11/11 |
Mid-term (同步輻射中心用戶會議) |
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第10週 |
11/18 |
Biophysical Methods to Probe Non-covalent Molecular Interaction (I):Circular Dichroism, UV and Fluorescence Spectroscopy |
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第11週 |
11/25 |
Biophysical Methods to Probe Non-covalent Molecular Interaction (II):Surface Plasmon Resonance, ITC and Analytical Ultracentrifugation |
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第12週 |
12/2 |
Structural Basis of Signal Transduction and Post-translation Modification |
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第13週 |
12/9 |
Molecular Enzymology |
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第14週 |
12/16 |
Protein/peptide interaction with membrane |
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第15週 |
12/23 |
Structural Features of Receptors and ligands |
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第16週 |
12/30 |
Structural View of Protein-DNA Recognition in Gene Regulation |
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第17週 |
1/6 |
Molecular Docking and Bioinformatics Approach:Strategies for Drug Discovery, Rational Drug Design versus Drug screen |
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第18週 |
1/13 |
(1) 12/02
黃詒敏
1. Shin D, Mukherjee R, Grewe D, Bojkova D, Baek K, Bhattacharya A, Schulz L, Widera M, Mehdipour AR, Tascher G, Geurink PP, Wilhelm A, van der Heden van Noort GJ, Ovaa H, Müller S, Knobeloch KP, Rajalingam K, Schulman BA, Cinatl J, Hummer G, Ciesek S, Dikic I. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature. 2020 Jul 29. doi: 10.1038/s41586-020-2601-5. Epub ahead of print. PMID: 32726803.
李冠緯
2. Zhang L, Lin D, Sun X, Curth U, Drosten C, Sauerhering L, Becker S, Rox K, Hilgenfeld R. Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved α-ketoamide inhibitors. Science. 2020 Apr 24;368(6489):409-412. doi: 10.1126/science.abb3405. Epub 2020 Mar 20. PMID: 32198291; PMCID: PMC7164518.
(2) 12/09
李政祐
3. Structures of a dimodular nonribosomal peptide synthetase reveal conformational flexibility. Reimer JM, Eivaskhani M, Harb I, Guarné A, Weigt M, Schmeing TM.
Science. 2019 Nov 8;366(6466):eaaw4388. doi: 10.1126/science.aaw4388.
林竺諼
4. Structures of two distinct conformations of holo-non-ribosomal peptide synthetases. Drake EJ, Miller BR, Shi C, Tarrasch JT, Sundlov JA, Allen CL, Skiniotis G, Aldrich CC, Gulick AM. Nature. 2016 Jan 14;529(7585):235-8. doi: 10.1038/nature16163.
(3) 12/16
何宗彥
5. Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates. Czekster, C.M., Ludewig, H., McMahon, S.A., Naismith, J.H. (2017) Nat Commun 8: 1045-1045
呂彥儒
6. Trapping conformational states of a flavin-dependent N -monooxygenase in crystallo reveals protein and flavin dynamics. Campbell, A.C., Stiers, K.M., Martin Del Campo, J.S., Mehra-Chaudhary, R., Sobrado, P., Tanner, J.J. (2020) J Biol Chem 295: 13239-13249
黃尉嘉
7. Structural basis for precursor protein-directed ribosomal peptide macrocyclization. Li, K., Condurso, H.L., Li, G., Ding, Y., Bruner, S.D. (2016) Nat Chem Biol 12: 973-979
(4)12/23
鄭光淳
Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication. Vuong W, Khan MB, Fischer C, Arutyunova E, Lamer T, Shields J, Saffran HA, McKay RT, van Belkum MJ, Joyce MA, Young HS, Tyrrell DL, Vederas JC, Lemieux MJ. Nat Commun. 2020 Aug 27;11(1):4282. doi: 10.1038/s41467-020-18096-2.
范宏綦
Hydrophobic and charged residues in the C-terminal arm of hepatitis C virus RNA-dependent RNA polymerase regulate initiation and elongation. Cherry AL, Dennis CA, Baron A, Eisele LE, Thommes PA, Jaeger J. J Virol. 2015 Feb;89(4):2052-63. doi: 10.1128/JVI.01106-14. Epub 2014 Nov 26.
劉佳容
Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Xia S, Liu M, Wang C, Xu W, Lan Q, Feng S, Qi F, Bao L, Du L, Liu S, Qin C, Sun F, Shi Z, Zhu Y, Jiang S, Lu L. Cell Res. 2020 Apr;30(4):343-355. doi: 10.1038/s41422-020-0305-x. Epub 2020 Mar 30.
(5) 12/30
陳奕伯
A β-Mannanase with a Lysozyme-like Fold and a Novel Molecular Catalytic Mechanism. Jin Y, Petricevic M, John A, Raich L, Jenkins H, Portela De Souza L, Cuskin F, Gilbert HJ, Rovira C, Goddard-Borger ED, Williams SJ, Davies GJ.
ACS Cent Sci. 2016 Dec 28;2(12):896-903. doi: 10.1021/acscentsci.6b00232. Epub 2016 Nov 8.
蘇筱晴
HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
Suskiewicz, M.J., Zobel, F., Ogden, T.E.H., Fontana, P., Ariza, A., Yang, J.C., Zhu, K., Bracken, L., Hawthorne, W.J., Ahel, D., Neuhaus, D., Ahel, I.
(2020) Nature 579: 598-602
廖小惟
Identification of a Class of Protein Adp-Ribosylating Sirtuins in Microbial Pathogens. Rack, J.G., Morra, R., Barkauskaite, E., Kraehenbuehl, R., Ariza, A., Qu, Y., Ortmayer, M., Leidecker, O., Cameron, D.R., Matic, I., Peleg, A.Y., Leys, D., Traven, A., Ahel, I.
(2015) Mol Cell 59: 309
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