博碩士論文 86345010 詳細資訊




以作者查詢圖書館館藏 以作者查詢臺灣博碩士 以作者查詢全國書目 勘誤回報 、線上人數:31 、訪客IP:3.139.233.17
姓名 吳立青(Li-Cheng Wu)  查詢紙本館藏   畢業系所 資訊工程學系
論文名稱 原核生物體內蛋白質熱穩定性之序列與結構特徵
(Structural and sequence features associated with protein thermostability in prokaryotic organisms: a bioinformatics study)
相關論文
★ 應用嵌入式系統於呼吸肌肉群訓練儀之系統開發★ 勃起障礙與缺血性心臟病的雙向研究: 以台灣全人口基礎的世代研究
★ 基質輔助雷射脫附飛行時間式串聯質譜儀 微生物抗藥性資料視覺化工具★ 使用穿戴式裝置分析心律變異及偵測心律不整之應用程式
★ 建立一個自動化分析系統用來分析任何兩種疾病之間的關聯性透過世代研究設計以及使用承保抽樣歸人檔★ 青光眼病患併發糖尿病,使用Metformin及Sulfonylurea治療得到中風之風險:以台灣人口為基礎的觀察性研究
★ 利用組成識別和序列及空間特性構成之預測系統來針對蛋白質交互作用上的特殊區段點位進行分析及預測辨識★ 新聞語意特徵擷取流程設計與股價變化關聯性分析
★ 藥物與疾病關聯性自動化分析平台設計與實作★ 建立財務報告自動分析系統進行股價預測
★ 建立一個分析疾病與癌症關聯性的自動化系統★ 基於慣性感測器虛擬鍵盤之設計與實作
★ 一個醫療照護監測系統之實作★ 應用手機開發手握球握力及相關資料之量測
★ 利用關聯分析全面性的搜索癌症關聯疾病★ 全面性尋找類風濕性關節炎之關聯疾病
檔案 [Endnote RIS 格式]    [Bibtex 格式]    [相關文章]   [文章引用]   [完整記錄]   [館藏目錄]   [檢視]  [下載]
  1. 本電子論文使用權限為同意立即開放。
  2. 已達開放權限電子全文僅授權使用者為學術研究之目的,進行個人非營利性質之檢索、閱讀、列印。
  3. 請遵守中華民國著作權法之相關規定,切勿任意重製、散佈、改作、轉貼、播送,以免觸法。

摘要(中) 新近的發展在對蛋白質的穩定的研究大多是根據在一些類似結構之間的蛋白質間的比較,並顯示增加樊得瓦爾相互作用力、氫鍵、鹽橋、或者偶極偶極相互作用對增加耐溫性有潛在的幫助。蛋白質Motif代表蛋白質群組內演化保存下來的區域,一般相信這些被保留的區域跟蛋白質的穩定和功能有關。 在一些類似結構之間的比較的方法或者部份物種的同源蛋白質比對以外,需要一個完整對當今的已知的蛋白質結構和序列上的耐溫性的分析。因為耐溫性分析需要蛋白質熱穩定的溫度資料,一個擁有蛋白質熱穩定資料的生物資料庫更是不可會缺的。在這篇論文裡,我們提出一個預測資訊系統,能對原核生物的結構蛋白質與蛋白質序列的熱穩定性做分析與預測。系統中包含一個原核生物最適生長溫度資料庫,命名為PGTdb。 對於已知結構的蛋白質,系統能對不同胺基酸所形成不同強度的離子對的數量做分析並且使用Bayesian classifier預測此蛋白質結構的熱穩定性。此預測系統對超耐熱蛋白質的預測準確度具有特別高的準確度。對只有序列沒有結構的蛋白質,系統在Pfam蛋白質群組之間做比較並找出有鑑別力的motif 區域。 系統成功找出一些被保留在部分蛋白質家族中具有鑑別力的溫度相關motif。研究案例顯示有鑑別力的motif與蛋白質的thermostability有關。最適的生長溫度資訊資料庫PGTdb在微生物的培養過程中非常有用,並且與很多生化物質的生產密切相關。 另外,在相應低溫和耐高溫蛋白質群組之間的比較提供與熱穩定性有關的關鍵生物化學的洞察力並且能用來測試蛋白質群組中個別結構上差異與演化的穩定性。
摘要(英) Recent developments in research on the stability of proteins show that thermophilic proteins generally have increased numbers of van der Waals interactions, hydrogen bonds, salt bridges, or dipole-dipole interaction potentially contribute to the thermostability of proteins, according to comparisons between some homologous structures. Protein motifs represent highly conserved regions within protein families and are generally accepted to describe critical regions required for protein stability and function. Beyond methods of comparisons between some homologous structures or limited number of genome, a complete analysis of the thermostability on current known protein structure and sequences is need. Since the thermostability analysis requires thermo-stable information of proteins, a biological database of thermo-stable information is crucial. In this Dissertation, we propose a predictive system which is capable of predicting thermostability of protein in prokaryotes and detecting discriminative motif occurrence on proteins of specific temperature, i.e., mesophilic or thermophilic. The system contains a database containing optimal growth temperatures of prokaryotic, namely PGTdb. For protein structure, the system can take input of ion-pair feature and predict the thermostability using Bayesian classifier base on ion-pair of known thermostability proteins. The prediction achieves high precision especially on hyperthermophilic protein structures. For protein sequences, the system identifies and compares corresponding mesophilic and thermophilic sequence motifs between Pfam protein families and conserved orthologous groups. The system successfully identifies some motif which only conserved on mesophilic or thermophilic sub-family but is not conserved on their counterpart sub-family. The case study shows that the discriminative motifs are related to thermostability of proteins. The optimal growth temperature information in PGTdb is very useful in cultivation of microbes, which is closely related to production of many biomaterials. Additionally, the comparisons between corresponding mesophilic and thermophilic protein families provide key biochemical insights related to thermostability and can be used to test the evolutionary robustness of individual structural comparisons of protein families.
關鍵字(中) ★ 熱穩定性
★ 蛋白質
★ 生物資訊
關鍵字(英) ★ Bioinformatics
★ Protein
★ Thermostability
論文目次 Table of Contents
摘要 V
ABSTRACT VI
致謝 VII
TABLE OF CONTENTS VIII
LIST OF FIGURES XII
LIST OF TABLES XV
CHAPTER 1 INTRODUCTION 1
1.1 BACKGROUND 3
1.1.1 The genome 3
1.1.2 DNA, RNA, and Protein 3
1.1.3 Amino acid 4
1.1.4 Peptides 6
1.1.5 Protein sequence 6
1.1.6 Protein structure 6
1.1.7 Protein thermostability 9
1.2 MOTIVATION 9
1.3 PROBLEM DESCRIPTION 11
1.3.1 A protein temperature database for studying protein thermostability 11
1.3.2 An integrated data source of temperature information for proteins 12
1.3.3 A prediction model of protein thermostability based on structure features 12
1.3.4 Analysis of relations of protein motif and protein thermostability 13
1.4 RELATED WORKS 13
1.4.1 Biological databases 13
1.4.2 Protein sequence databases 14
1.4.3 Protein motif and motif discovery 14
1.4.4 Protein family 15
1.4.5 Pfam: protein families database of alignments and HMMs 16
1.4.6 Protein and gene family database COG: clusters of orthologous groups 16
1.4.7 ProTherm 17
1.4.8 Sequence alignment 18
1.4.9 HMMER: profile HMMs for protein sequence analysis 19
1.4.10 Data warehousing system 19
1.4.11 Bayesian Network 21
1.5 RESEARCH GOALS 22
1.6 ORGANIZATION OF THIS DISSERTATION 25
CHAPTER 2 PGTDB-THE PROKARYOTIC GROWTH TEMPERATURE DATABASE 26
2.1 THE OPTIMAL GROWTH TEMPERATURE 26
2.2 ORGANIZATION AND CONTENTS OF THE DATABASE 28
2.2.1 Organization of the database 28
2.2.2 Content and relations of the database 29
2.2.3 Data origination of the database 31
2.2.4 Reference to other databases 31
2.2.5 Protein family information 33
2.2.6 Protein family alignment 34
2.2.7 Amino acid composition of a protein family 35
2.2.8 Data base query interface construction 35
2.3 APPLICATIONS 36
2.3.1 Cultivation of microbes 36
2.3.2 Protein engineering 36
2.3.3 Physiology and ecology 37
2.4 SUMMARY 37
CHAPTER 3 A PROBABILISTIC METHOD TO CORRELATE ION-PAIRS TO PROTEIN THERMOSTABILITY 38
3.1 A PROBABILISTIC METHOD 38
3.1.1 Material 38
3.1.2 Structure features 39
3.1.3 Naïve Bayesian classifier 40
3.1.4 Prediction using naïve Bayesian classifier 41
3.2 CORRELATE ION-PAIRS TO PROTEIN THERMOSTABILITY RESULTS 43
3.2.1 Result measurement 43
3.2.2 Result of 3 functional families: α-amylase, GAPDH, and Xylanase 46
3.2.3 Result of functional family: Xylanase 48
3.3 SUMMARY 49
CHAPTER 4 DETECTION OF DISCRIMINATIVE SEQUENCE MOTIFS FROM PROKARYOTES GROWN AT VARIOUS TEMPERATURES 51
4.1 DETECTION OF DISCRIMINATIVE SEQUENCE MOTIFS 51
4.1.1 System flow 51
4.1.2 Motif discovery 52
4.1.3 Motif model construction 52
4.1.4 Motif model matching 53
4.1.5 Statistical test 53
4.2 DISCRIMINATIVE MOTIF RESULTS 55
4.2.1 Discriminative motif of Pfam families 55
4.2.2 Discriminative motif of COGs 57
4.2.3 Match ratio of Pfam families 58
4.2.4 Match ratio of COG families 61
4.2.5 Association with protein structure 64
4.2.6 Amino acid composition 65
4.3 SUMMARY 66
CHAPTER 5 CASE STUDIES 67
5.1 CASE STUDY OF GAPDH 67
5.1.1 Thermostability prediction 67
5.1.2 Discriminative motif 68
5.1.3 Amino acid composition 72
5.2 CASE STUDY OF TRIOSEPHOSPHATE ISOMERASE 73
5.2.1 Discriminative motif 73
5.2.2 Amino acid composition 74
5.3 CASE STUDY OF THIOREDOXIN 75
5.3.1 Discriminative motif 75
5.3.2 Amino acid composition 76
CHAPTER 6 DISCUSSIONS 78
6.1 CHARACTERISTIC OF THE SYSTEM 78
6.2 A COMPARISON TO OTHER SYSTEMS 79
CHAPTER 7 CONCLUSION 82
REFERENCES 84
APPENDIX 90
參考文獻 Andreeva, A., Howorth, D., Brenner, S.E., Hubbard, T.J., Chothia, C., and Murzin, A.G. 2004. SCOP database in 2004: refinements integrate structure and sequence family data. Nucleic Acids Res 32, D226-229.
Apweiler, R. et al. 2004. UniProt: the Universal Protein knowledgebase. Nucleic Acids Res 32, D115-119.
Attwood, T.K., Beck, M.E., Bleasby, A.J., Degtyarenko, K., Michie, A.D., and Parry-Smith, D.J. 1997. Novel developments with the PRINTS protein fingerprint database. Nucleic Acids Res 25, 212-217.
Bailey, T.L. and Elkan, C. 1994. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc Int Conf Intell Syst Mol Biol 2, 28-36.
Bailey, T.L. and Gribskov, M. 1998. Methods and statistics for combining motif match scores. J Comput Biol 5, 211-221.
Bairoch, A. 1992. PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res 20, 2013-2018.
Bairoch, A. 1999. The ENZYME data bank in 1999. Nucleic Acids Res 27, 310-311.
Barker, W.C. et al. 2000. The protein information resource (PIR). Nucleic Acids Res 28, 41-44.
Barlow, D.J. and Thornton, J.M. 1983. Ion-pairs in proteins. J Mol Biol 168, 867-885.
Bateman, A. et al. 2004. The Pfam protein families database. Nucleic Acids Res 32, D138-141.
Benson, D.A., Karsch-Mizrachi, I., Lipman, D.J., Ostell, J., and Wheeler, D.L. 2003. GenBank. Nucleic Acids Res 31, 23-27.
Berman, H.M. et al. 2002. The Protein Data Bank. Acta Crystallogr D Biol Crystallogr 58, 899-907.
Boeckmann, B. et al. 2003. The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res 31, 365-370.
Bolon, D.N. and Mayo, S.L. 2001. Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity. Biochemistry 40, 10047-10053.
Branden, C. and Tooze, J. 1991. Introduction to Protein Structure. Garland Publishing Inc.
Burton, S.G. 2003. Oxidizing enzymes as biocatalysts. Trends Biotechnol 21, 543-549.
Chakrabarti, A., Srivastava, S., Swaminathan, C.P., Surolia, A., and Varadarajan, R. 1999. Thermodynamics of replacing an alpha-helical Pro residue in the P40S mutant of Escherichia coli thioredoxin. Protein Sci 8, 2455-2459.
Chakravarty, S. and Varadarajan, R. 2002. Elucidation of factors responsible for enhanced thermal stability of proteins: a structural genomics based study. Biochemistry 41, 8152-8161.
Cooper, G. 1989. Current Research Directions in The Development of Expert Systems Based on Belief Networks. Applied Stochastic Models and Data Analysis 5, 39-52.
Corpet, F., Servant, F., Gouzy, J., and Kahn, D. 2000. ProDom and ProDom-CG: tools for protein domain analysis and whole genome comparisons. Nucleic Acids Res 28, 267-269.
Ding, Y. and Lawrence, C.E. 1999. A bayesian statistical algorithm for RNA secondary structure prediction. Comput Chem 23, 387-400.
Dror, O., Benyamini, H., Nussinov, R., and Wolfson, H. 2003. MASS: multiple structural alignment by secondary structures. Bioinformatics 19, i95-104.
Durbin, R., Eddy, S., Krogh, A., and Mitchison, G. 1998. Biological Sequence Analysis: Probabilistic Models of Proteins and Nucleic Acids. Cambridge University Press,.
Feinstein, A.R. 1977. Clinical biostatistics. XXXIX. The haze of Bayes, the aerial palaces of decision analysis, and the computerized Ouija board. Clin Pharmacol Ther 21, 482-496.
Frankes, W.B. and Baeza-Yates, R. 1992. Information retrieval: data structures and algorithms. Prentice-Hall, Inc., Upper Saddle River, NJ, USA.
Friedman, N., Linial, M., Nachman, I., and Pe'er, D. 2000. Using Bayesian networks to analyze expression data. J Comput Biol 7, 601-620.
Fukuchi, S. and Nishikawa, K. 2001. Protein surface amino acid compositions distinctively differ between thermophilic and mesophilic bacteria. J Mol Biol 309, 835-843.
Gracia, M.I., Latorre, M.A., Garcia, M., Lazaro, R., and Mateos, G.G. 2003. Heat processing of barley and enzyme supplementation of diets for broilers. Poult Sci 82, 1281-1291.
Gracy, J. and Argos, P. 1998. DOMO: a new database of aligned protein domains. Trends Biochem Sci 23, 495-497.
Gromiha, M.M., Oobatake, M., and Sarai, A. 1999. Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophys Chem 82, 51-67.
Gromiha, M.M., Uedaira, H., An, J., Selvaraj, S., Prabakaran, P., and Sarai, A. 2002. ProTherm, Thermodynamic Database for Proteins and Mutants: developments in version 3.0. Nucleic Acids Res 30, 301-302.
Guex, N. and Peitsch, M.C. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
Hatzivassiloglou, V., Duboue, P.A., and Rzhetsky, A. 2001. Disambiguating proteins, genes, and RNA in text: a machine learning approach. Bioinformatics 17, S97-106.
Holte, R.C. 1993. Very Simple Classification Rules Perform Well on Most Commonly Used Dataset. In Machine Learning, pp. 63-91.
Horng, J.T., Hu, K.C., Wu, L.C., Huang, H.D., Lin, F.M., Huang, S.L., Lai, H.C., and Chu, T.Y. 2004. Identifying the combination of genetic factors that determine susceptibility to cervical cancer. IEEE Trans Inf Technol Biomed 8, 59-66.
Horng, J.T., Huang, H.D., Wang, S.H., Chen, M.Y., Huang, S.L., and Hwang, J.K. 2003. Computing motif correlations in proteins. J Comput Chem 24, 2032-2043.
Huang, S.L., Wu, L.C., Huang, H.D., Liang, H.K., Ko, M.T., and Horng, J.T. 2004a. A probabilistic method to correlate ion pairs with protein thermostability. Applied Bioinfomatics 3, 21-29.
Huang, S.L., Wu, L.C., Liang, H.K., Pan, K.T., Horng, J.T., and Ko, M.T. 2004b. PGTdb: a database providing growth temperatures of prokaryotes. Bioinformatics 20, 276-278.
Jaenicke, R. and Bohm, G. 1998. The stability of proteins in extreme environments. Curr Opin Struct Biol 8, 738-748.
Jaenicke, R. and Bohm, G. 2001. Thermostability of proteins from Thermotoga maritima. Methods Enzymol 334, 438-469.
Jansen, R. et al. 2003. A Bayesian networks approach for predicting protein-protein interactions from genomic data. Science 302, 449-453.
Jensen, F. 1996. An Introduction to Bayesian Networks. Springer Verlag, New York.
Kataeva, I.A., Blum, D.L., Li, X.L., and Ljungdahl, L.G. 2001. Do domain interactions of glycosyl hydrolases from Clostridium thermocellum contribute to protein thermostability? Protein Eng 14, 167-172.
Kelley, R.F. and Richards, F.M. 1987. Replacement of proline-76 with alanine eliminates the slowest kinetic phase in thioredoxin folding. Biochemistry 26, 6765-6774.
Klappenbach, J.A., Saxman, P.R., Cole, J.R., and Schmidt, T.M. 2001. rrndb: the Ribosomal RNA Operon Copy Number Database. Nucleic Acids Res 29, 181-184.
Kreil, D.P. and Ouzounis, C.A. 2001. Identification of thermophilic species by the amino acid compositions deduced from their genomes. Nucleic Acids Res 29, 1608-1615.
Krogh, A., Brown, M., Mian, I.S., Sjolander, K., and Haussler, D. 1994. Hidden Markov models in computational biology. Applications to protein modeling. J Mol Biol 235, 1501-1531.
Kumar, S. and Nussinov, R. 1999. Salt bridge stability in monomeric proteins. J Mol Biol 293, 1241-1255.
Kumar, S. and Nussinov, R. 2001. How do thermophilic proteins deal with heat? Cell Mol Life Sci 58, 1216-1233.
Kumar, S., Tsai, C.J., and Nussinov, R. 2000. Factors enhancing protein thermostability. Protein Eng 13, 179-191.
La, D., Silver, M., Edgar, R.C., and Livesay, D.R. 2003. Using motif-based methods in multiple genome analyses: a case study comparing orthologous mesophilic and thermophilic proteins. Biochemistry 42, 8988-8998.
Ladbury, J.E., Wynn, R., Thomson, J.A., and Sturtevant, J.M. 1995. Substitution of charged residues into the hydrophobic core of Escherichia coli thioredoxin results in a change in heat capacity of the native protein. Biochemistry 34, 2148-2152.
Lebbink, J.H., Knapp, S., van der Oost, J., Rice, D., Ladenstein, R., and de Vos, W.M. 1999. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface. J Mol Biol 289, 357-369.
Levashov, P., Orlov, V., Boschi-Muller, S., Talfournier, F., Asryants, R., Bulatnikov, I., Muronetz, V., Branlant, G., and Nagradova, N. 1999. Thermal unfolding of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase studied by differential scanning calorimetry. Biochim Biophys Acta 1433, 294-306.
Lin, T.Y. and Kim, P.S. 1991. Evaluating the effects of a single amino acid substitution on both the native and denatured states of a protein. Proc Natl Acad Sci U S A 88, 10573-10577.
Lubert, S. 1995. Biochemistry. W.H. Freeman Press, New York.
Michael T. Madigan, J.M.M. and Parker, J. 2000. Brock Biology of Microorganisms. Prentice-Hall Inc., New Jersey.
Mitchell, T. 1997. Machine Learning. Mcgraw-Hill Companies, NewYork.
Mulder, N.J. et al. 2003. The InterPro Database, 2003 brings increased coverage and new features. Nucleic Acids Res 31, 315-318.
Nicastro, G., De Chiara, C., Pedone, E., Tato, M., Rossi, M., and Bartolucci, S. 2000. NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability. Eur J Biochem 267, 403-413.
Onuchic, J.N., Luthey-Schulten, Z., and Wolynes, P.G. 1997. Theory of protein folding: the energy landscape perspective. Annu Rev Phys Chem 48, 545-600.
Orengo, C.A., Pearl, F.M., and Thornton, J.M. 2003. The CATH domain structure database. Methods Biochem Anal 44, 249-271.
Pearson, W.R. and Lipman, D.J. 1988. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A 85, 2444-2448.
Pedone, E., Cannio, R., Saviano, M., Rossi, M., and Bartolucci, S. 1999. Prediction and experimental testing of Bacillus acidocaldarius thioredoxin stability. Biochem J 339, 309-317.
Pedone, E., Saviano, M., Rossi, M., and Bartolucci, S. 2001. A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli. Protein Eng 14, 255-260.
Peter H. A. Sneath, Nicholas S. Mair, Sharpe, M.E., and Holt, J.G. 1986. Bergey's Manual of Systematic Bacteriology. Williams & Wilkins: A Waverly Company.
Qu, K., McCue, L.A., and Lawrence, C.E. 1998. Bayesian protein family classifier. Proc Int Conf Intell Syst Mol Biol 6, 131-139.
Roitel, O., Ivinova, O., Muronetz, V., Nagradova, N., and Branlant, G. 2002. Thermal unfolding used as a probe to characterize the intra- and intersubunit stabilizing interactions in phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. Biochemistry 41, 7556-7564.
Servant, F., Bru, C., Carrere, S., Courcelle, E., Gouzy, J., Peyruc, D., and Kahn, D. 2002. ProDom: automated clustering of homologous domains. Brief Bioinform 3, 246-251.
Silverstein, K.A., Shoop, E., Johnson, J.E., and Retzel, E.F. 2001. MetaFam: a unified classification of protein families. I. Overview and statistics. Bioinformatics 17, 249-261.
Szilagyi, A. and Zavodszky, P. 2000. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure Fold Des 8, 493-504.
T.Madigan, M., Martinko, J.M., and Parker, J. 2000. Brock Biology of Microorganisms. Prentice-Hall Inc., New Jersey.
Tatusov, R.L. et al. 2003. The COG database: an updated version includes eukaryotes. BMC Bioinformatics 4, 41.
Tatusov, R.L., Galperin, M.Y., Natale, D.A., and Koonin, E.V. 2000. The COG database: a tool for genome-scale analysis of protein functions and evolution. Nucleic Acids Res 28, 33-36.
Tatusov, R.L., Koonin, E.V., and Lipman, D.J. 1997. A genomic perspective on protein families. Science 278, 631-637.
Tatusov, R.L. et al. 2001. The COG database: new developments in phylogenetic classification of proteins from complete genomes. Nucleic Acids Res 29, 22-28.
Thompson, W., Rouchka, E.C., and Lawrence, C.E. 2003. Gibbs Recursive Sampler: finding transcription factor binding sites. Nucleic Acids Res 31, 3580-3585.
Vieille, C. and Zeikus, G.J. 2001. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65, 1-43.
Vogt, G., Woell, S., and Argos, P. 1997. Protein thermal stability, hydrogen bonds, and ion pairs. J Mol Biol 269, 631-643.
Voronov, S., Zueva, N., Orlov, V., Arutyunyan, A., and Kost, O. 2002. Temperature-induced selective death of the C-domain within angiotensin-converting enzyme molecule. FEBS Lett 522, 77-82.
Wackerly, D.D., III, W.M., and Scheaffer, R.L. 1996. Mathematical Statistics with Applications. Duxbury Press, New York.
Wu, C.H., Huang, H., Nikolskaya, A., Hu, Z., and Barker, W.C. 2004. The iProClass integrated database for protein functional analysis. Comput Biol Chem 28, 87-96.
Wu, C.H., Huang, H., Yeh, L.S., and Barker, W.C. 2003. Protein family classification and functional annotation. Comput Biol Chem 27, 37-47.
Wu, C.H., Xiao, C., Hou, Z., Huang, H., and Barker, W.C. 2001. iProClass: an integrated, comprehensive and annotated protein classification database. Nucleic Acids Res 29, 52-54.
Yona, G., Linial, N., and Linial, M. 2000. ProtoMap: automatic classification of protein sequences and hierarchy of protein families. Nucleic Acids Res 28, 49-55.
Zdobnov, E.M. and Apweiler, R. 2001. InterProScan--an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17, 847-848.
Zhu, J., Liu, J.S., and Lawrence, C.E. 1998. Bayesian adaptive sequence alignment algorithms. Bioinformatics 14, 25-39.
指導教授 黃雪莉、洪炯宗
(Shir-Ly Huang、Jorng-Tzong Horng)
審核日期 2004-7-14
推文 facebook   plurk   twitter   funp   google   live   udn   HD   myshare   reddit   netvibes   friend   youpush   delicious   baidu   
網路書籤 Google bookmarks   del.icio.us   hemidemi   myshare   

若有論文相關問題,請聯絡國立中央大學圖書館推廣服務組 TEL:(03)422-7151轉57407,或E-mail聯絡  - 隱私權政策聲明