甲型流感病毒蛋白質(zhì)空間結(jié)構(gòu)預測
發(fā)布時間：2018-08-25 16:49
【摘要】：甲型流感病毒具有極強的變異性，是歷史上導致病患死亡人數(shù)最多的流行病毒之一。每一次甲型流感大爆發(fā)都是由其變異得到的新亞型和之前出現(xiàn)過的亞型流感病毒再次出現(xiàn)而引起。自20世紀以來，歷史上共發(fā)生四次較大規(guī)模的流感病毒大流行，其每一次都對人類公共衛(wèi)生和社會經(jīng)濟發(fā)展造成極大的破壞，因此對甲型流感病毒的研究已逐漸成為眾多研究者的重要研究方向。目前對甲型流感病毒的研究主要是關于其DNA、RNA和蛋白質(zhì)序列，從生物化學、生物物理學以及統(tǒng)計學等多角度去研究其序列的變化情況，并找到其中的變化規(guī)律。 文章首先介紹了最近甲型流感病毒的變異和流行情況，以其10種組成蛋白作為研究對象，在NCBI數(shù)據(jù)庫中獲得1902-2013年間關于甲型流感病毒10種組成蛋白的所有氨基酸序列，利用MATLAB進行大數(shù)據(jù)編程分析，結(jié)合詳細的HP模型，并基于CGR-Walk模型將全部甲型流感病毒蛋白質(zhì)序列轉(zhuǎn)化為數(shù)據(jù)形式，引入時間序列ARFIMA(p,d,q)模型擬合所有數(shù)據(jù)化序列，分析10種組成蛋白的序列在1902-2013年間的變化趨勢，并進一步對其未來10年的發(fā)展趨勢進行預測。然后以甲型流感病毒蛋白質(zhì)氨基酸序列變化規(guī)律的研究作為基礎，運用從頭計算的思想選擇甲型H1N1流感病毒的蛋白質(zhì)作為研究對象對其空間結(jié)構(gòu)進行研究�；诘鞍踪|(zhì)空間結(jié)構(gòu)的HP模型，文中構(gòu)建了甲型H1N1流感病毒蛋白質(zhì)空間結(jié)構(gòu)的3DHP模型，并利用優(yōu)化的遺傳算法找到具有最小自由能的優(yōu)化結(jié)構(gòu)，從而對甲型H1N1流感病毒蛋白質(zhì)三維空間結(jié)構(gòu)進行初步模建預測。之后鑒于HP格點模型過于簡單，則根據(jù)甲型H1N1流感病毒的典型病毒顆粒呈球狀這一特性，，利用這樣的球狀結(jié)構(gòu)中氨基酸殘基間形成的緊密接觸對的能力不同，將20種氨基酸分成四類，并得到HNXP三維空間格點模型。采用優(yōu)化的遺傳算法得到其自由能最小的蛋白質(zhì)HNXP三維空間結(jié)構(gòu)，并采用稀疏典型相關性分析法將模建得到的結(jié)構(gòu)與真實蛋白質(zhì)空間結(jié)構(gòu)進行對比分析，經(jīng)檢驗得兩者在結(jié)構(gòu)上高度相似。 本文利用組成其序列的20種氨基酸之間所包含的生物信息對甲型流感病毒的三維空間結(jié)構(gòu)進行預測，將目前關于甲型流感病毒對蛋白質(zhì)氨基酸序列的研究進一步拓展至三維。研究結(jié)果可為甲型流感病毒蛋白質(zhì)氨基酸序列空間結(jié)構(gòu)的預測提供借鑒。
[Abstract]:Influenza A virus is one of the most prevalent viruses with the highest number of deaths in history. Each outbreak of influenza A is caused by the reappearance of new subtypes and previous subtypes of influenza viruses. Since the 20th century, there have been four large-scale pandemics of influenza viruses, each of which has caused great damage to human public health and socio-economic development. Therefore, the study of influenza A virus has gradually become an important research direction of many researchers. At present, the study of influenza A virus is mainly about its DNA,RNA and protein sequences. The changes of the sequences are studied from the aspects of biochemistry, biophysics and statistics, and the changing rules are found. This paper first introduces the variation and prevalence of influenza A virus recently. Taking its 10 constituent proteins as the research object, all the amino acid sequences of 10 components of influenza A virus from 1902 to 2013 were obtained in NCBI database. Big data programming analysis was carried out with MATLAB, combined with the detailed HP model, and based on the CGR-Walk model, all the protein sequences of influenza A virus were transformed into data form, and the time series ARFIMA model was introduced to fit all the digitized sequences. The variation trend of 10 kinds of protein sequences from 1902 to 2013 was analyzed, and the trend of development in the next 10 years was forecasted. Based on the study of amino acid sequence variation of influenza A virus protein, the spatial structure of influenza A H1N1 virus was studied by ab initio method. Based on the HP model of protein spatial structure, the 3DHP model of protein spatial structure of A H1N1 influenza virus is constructed, and the optimized structure with minimum free energy is found by using the optimized genetic algorithm. Thus the three-dimensional spatial structure of influenza A H1N1 virus protein was predicted. Then, given that the HP lattice model is too simple, the ability to make use of the tight contact pairs formed between amino acid residues in such a spherical structure is different according to the characteristic that the typical virus particles of A / H1N1 influenza virus are spherical. The 20 amino acids were divided into four classes and the HNXP three dimensional lattice model was obtained. The three-dimension structure of protein HNXP with minimal free energy was obtained by using the optimized genetic algorithm, and the structure of the model was compared with that of the real protein by sparse canonical correlation analysis. It has been tested that the two are highly similar in structure. In this paper, the three-dimensional structure of influenza A virus is predicted by the biological information contained among the 20 amino acids that make up its sequence, and the current research on the amino acid sequence of protein of influenza A virus is further expanded to three dimensions. The results can be used for prediction of amino acid sequence spatial structure of influenza A virus protein.
【學位授予單位】：江南大學
【學位級別】：碩士
【學位授予年份】：2014
【分類號】：R373;O175
本文編號：2203514
[Abstract]:Influenza A virus is one of the most prevalent viruses with the highest number of deaths in history. Each outbreak of influenza A is caused by the reappearance of new subtypes and previous subtypes of influenza viruses. Since the 20th century, there have been four large-scale pandemics of influenza viruses, each of which has caused great damage to human public health and socio-economic development. Therefore, the study of influenza A virus has gradually become an important research direction of many researchers. At present, the study of influenza A virus is mainly about its DNA,RNA and protein sequences. The changes of the sequences are studied from the aspects of biochemistry, biophysics and statistics, and the changing rules are found. This paper first introduces the variation and prevalence of influenza A virus recently. Taking its 10 constituent proteins as the research object, all the amino acid sequences of 10 components of influenza A virus from 1902 to 2013 were obtained in NCBI database. Big data programming analysis was carried out with MATLAB, combined with the detailed HP model, and based on the CGR-Walk model, all the protein sequences of influenza A virus were transformed into data form, and the time series ARFIMA model was introduced to fit all the digitized sequences. The variation trend of 10 kinds of protein sequences from 1902 to 2013 was analyzed, and the trend of development in the next 10 years was forecasted. Based on the study of amino acid sequence variation of influenza A virus protein, the spatial structure of influenza A H1N1 virus was studied by ab initio method. Based on the HP model of protein spatial structure, the 3DHP model of protein spatial structure of A H1N1 influenza virus is constructed, and the optimized structure with minimum free energy is found by using the optimized genetic algorithm. Thus the three-dimensional spatial structure of influenza A H1N1 virus protein was predicted. Then, given that the HP lattice model is too simple, the ability to make use of the tight contact pairs formed between amino acid residues in such a spherical structure is different according to the characteristic that the typical virus particles of A / H1N1 influenza virus are spherical. The 20 amino acids were divided into four classes and the HNXP three dimensional lattice model was obtained. The three-dimension structure of protein HNXP with minimal free energy was obtained by using the optimized genetic algorithm, and the structure of the model was compared with that of the real protein by sparse canonical correlation analysis. It has been tested that the two are highly similar in structure. In this paper, the three-dimensional structure of influenza A virus is predicted by the biological information contained among the 20 amino acids that make up its sequence, and the current research on the amino acid sequence of protein of influenza A virus is further expanded to three dimensions. The results can be used for prediction of amino acid sequence spatial structure of influenza A virus protein.
【學位授予單位】：江南大學
【學位級別】：碩士
【學位授予年份】：2014
【分類號】：R373;O175
【參考文獻】
相關期刊論文 前3條
1 王向紅,章林溪,趙得祿;蛋白質(zhì)分子的HNP格點模型[J];高分子學報;2004年02期
2 王革非;李康生;;新世紀流感大流行的思考[J];生物化學與生物物理進展;2009年08期
3 張玲;高潔;;甲型H1N1流感病毒蛋白質(zhì)序列的預測[J];生物技術(shù);2012年06期
本文編號：2203514
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