基于分子生物信息学分析小麦球蛋白的理化特性与结构预测
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摘要
为探讨小麦球蛋白在理化特性及分子结构方面的共性与特性,基于NCBI蛋白质数据库,利用Protparam、Clustalw、MEME program3、PSIPRED 3.3等软件对8条小麦球蛋白的理化性质、多序列比对、系统进化树、保守基序、蛋白质二级结构、域结构、折叠域识别等进行预测分析。结果表明:小麦球蛋白的氨基酸残基数为225～637,分子质量为24.55～72.25 kDa,理论等电点为5.22～8.72,总平均亲水性为-1.074～0.045,不稳定系数为36.02～77.64,脂肪系数为57.05～96.09。在多序列比对方面,小麦球蛋白存在较多保守区域;在基序分析方面,小麦球蛋白中有6个保守的基序;在结构预测方面,小麦球蛋白的域结构和折叠域差异较小;在蛋白质二级结构方面,氨基酸残基在225～241之间的小麦球蛋白由α-螺旋和无规则卷曲等结构元件组成,基本上不存在延伸链;氨基酸残基在504～637之间的小麦球蛋白则由α-螺旋、延伸链和无规则卷曲等结构元件组成,且三者的比例约为无规则卷曲∶延伸链∶α-螺旋=3∶1∶1。这些结果可为小麦球蛋白的分离纯化及其利用提供生物学数据参考。
In order to explore the commonness and characteristics of wheat globulins in physicochemical properties and molecular structures,the physicochemical properties,multiple sequence alignments phylogenetic trees,conserved motifs,protein folding domain recognition and protein secondary structures of eight wheat globulins were analyzed by bioinformatics softwares including Protparam,Clustalw,MEME program3,and PSIPRED version 3.3 based on the existing NCBI protein database in present study. The results showed that the amino acid numbers of analyzed proteins ranged from 225 to 637 aa. The molecular weight distribution varied from 24.55 to 72.25 kDa. The theoretical isoelectric points were range of 5.22 to 8.72. The average hydrophilicities were the scope of-1.774 to 0.045. The coefficients of instability were varying from 36.02 to77.64. The fat coefficients were the extent of 57.05 to 96.09. There were some conserved regions in multiple sequence alignments of wheat globulins,and six very conserved motifs in wheat globulins. The domain structure and folding domain structure of wheat globulins were less different. The secondary structures of wheat globulins(225～241 aa) were mainly composed of α-helices and random coils,and nearly nonexistent extended chains.However,the secondary structures of long wheat globulins(504～637 aa) were composed of α-helices,extended chains and random coils,as well as the ratio of the random coils,extended chains and α-helices was approximately 3 ∶1 ∶1. These results could provide biological data reference for the isolation,purification and utilization of wheat globulins.
In order to explore the commonness and characteristics of wheat globulins in physicochemical properties and molecular structures,the physicochemical properties,multiple sequence alignments phylogenetic trees,conserved motifs,protein folding domain recognition and protein secondary structures of eight wheat globulins were analyzed by bioinformatics softwares including Protparam,Clustalw,MEME program3,and PSIPRED version 3.3 based on the existing NCBI protein database in present study. The results showed that the amino acid numbers of analyzed proteins ranged from 225 to 637 aa. The molecular weight distribution varied from 24.55 to 72.25 kDa. The theoretical isoelectric points were range of 5.22 to 8.72. The average hydrophilicities were the scope of-1.774 to 0.045. The coefficients of instability were varying from 36.02 to77.64. The fat coefficients were the extent of 57.05 to 96.09. There were some conserved regions in multiple sequence alignments of wheat globulins,and six very conserved motifs in wheat globulins. The domain structure and folding domain structure of wheat globulins were less different. The secondary structures of wheat globulins(225～241 aa) were mainly composed of α-helices and random coils,and nearly nonexistent extended chains.However,the secondary structures of long wheat globulins(504～637 aa) were composed of α-helices,extended chains and random coils,as well as the ratio of the random coils,extended chains and α-helices was approximately 3 ∶1 ∶1. These results could provide biological data reference for the isolation,purification and utilization of wheat globulins.
引文
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[23]孙董董,林春花,李博勋,等. 3种炭疽菌P型ATP酶基因家族分析[J].热带作物学报,2015,36(4):737-745.
[24] XI J,CHEN J,XU M,et al. The polymorphisms of LCR,E6,and E7 of HPV-58 isolates in Yunnan,Southwest China[J]. Virology Journal,2018,15(1):76-83.
[2]刁大鹏,黄继红,李锦,等.小麦胚芽球蛋白提取工艺及分子质量测定[J].河南工业大学学报(自然科学版),2013,34(2):52-55.
[3] DEBITON C,MERLINO M,CHAMBON C,et al.Analyses of albumins,globulins and amphiphilic proteins by proteomic approach give new insights on waxy wheat starch metabolism[J]. Journal of Cereal Science,2011,53(2):160-169.
[4]况伟,王金水,卞科,等.面团搅拌过程中蛋白质变化的研究Ⅰ.清蛋白与球蛋白的变化规律[J].郑州工程学院学报,2002,23(4):5-7.
[5]张滨,于国莉,张颐骏,等.小麦盐溶蛋白组分韦恩分类及对馒头结构品质的影响[J].河南工业大学学报(自然科学版),2018,39(2):20-24.
[6]朱科学,周惠明.小麦胚8S球蛋白的分离纯化及理化性质研究[J].食品科学,2008,29(5):45-48.
[7]周显青,张玉荣,周玉珍,等.小麦胚球蛋白提取工艺的研究[J].食品工业科技,2005,26(8):128-131.
[8]朱科学,郭晓娜,彭伟,等.采用Raman光谱研究小麦胚芽8S球蛋白的二级结构[J].食品科学,2009,30(19):32-34.
[9]王正华,王勇献.后基因组时代生物信息学的新进展[J].国防科技大学学报,2003,25(1):1-6.
[10]吴清发.基因组学研究中一些常用软件的概述[J].遗传,2003,25(6):708-712.
[11]郭俊恩,王士同,徐红林.一种识别蛋白质的保守氨基酸残基的新方法[J].食品与生物技术学报,2007,26(5):38-43.
[12]高世杰,窦永喜,田波.基因组及蛋白质组学研究[J].动物医学进展,2005,26(4):107-110.
[13]马袁君,程震龙,孙野青.生物信息学及其在蛋白质组学中的应用[J].生物信息学,2008,6(1):38-39.
[14]程甜,郝志强,魏强,等.细菌萜类合成酶的生物信息学分析[J].微生物学通报,2015,42(10):1877-1887.
[15]熊辉岩,张超,多杰措,等.大麦HD-ZipⅣ基因家族的生物信息学分析[J].分子植物育种,2018(2):352-361.
[16]史松昌,张如月,赵振廷,等.谷子DREBs亚家族的全基因组学分析[J].基因组学与应用生物学,2018,37(2):827-835.
[17]李傲,崔梦杰,刘众杰,等.葡萄基因组无内含子基因生物信息学及其表达分析[J].南京农业大学学报,2018,41(4):655-661.
[18]向贵生.蔷薇科植物MLO蛋白家族的生物信息学分析[J].基因组学与应用生物学,2018,37(5):2043-2059.
[19]李闯,许笑蒙,李博,等.小麦锈菌蛋白激酶基因家族的鉴定与生物信息学分析[J].植物保护学报,2018(1):53-59.
[20]张琳,曹健,陈金鹏.微生物亚油酸异构酶的生物信息学分析[J].河南工业大学学报(自然科学版),2007,28(2):55-59.
[21] FLYNN E M,HUANG O W,POY F,et al. A subset of human bromodomains recognizes butyryllysine and crotonyllysine histone peptide modifications[J]. Structure,2015,23(10):1801-1814.
[22] LI F M,GAI X M. Phylogenetic analysis of cystatin[J].Agricultural Science&Technology,2010(2):37-39,43.
[23]孙董董,林春花,李博勋,等. 3种炭疽菌P型ATP酶基因家族分析[J].热带作物学报,2015,36(4):737-745.
[24] XI J,CHEN J,XU M,et al. The polymorphisms of LCR,E6,and E7 of HPV-58 isolates in Yunnan,Southwest China[J]. Virology Journal,2018,15(1):76-83.
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