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双峰驼凝乳酶原基因的生物信息学分析
引用本文:杨艺,普燕,张富春. 双峰驼凝乳酶原基因的生物信息学分析[J]. 生物信息学, 2014, 12(1): 18-26
作者姓名:杨艺  普燕  张富春
作者单位:新疆大学生命科学与技术学院,新疆生物资源与基因工程重点实验室,新疆,乌鲁木齐,830046;新疆大学生命科学与技术学院,新疆生物资源与基因工程重点实验室,新疆,乌鲁木齐,830046;新疆大学生命科学与技术学院,新疆生物资源与基因工程重点实验室,新疆,乌鲁木齐,830046
基金项目:新疆动物学重点学科-乳品工程资助(2011001)。
摘    要:通过生物信息学的方法对双峰驼凝乳酶原基因及相应的氨基酸序列的同源性、理化性质、保守结构域、亚细胞定位、信号肽、跨膜结构域、亲水性/疏水性、二级结构进行预测分析.结果表明,双峰驼凝乳酶原基因开放阅读框全长1 146 bp,编码381个氨基酸,属于胃蛋白酶A超家族,预测定位于内质网(膜)的稳定亲水性蛋白,具有一个16个氨基酸的信号肽,其不含跨膜结构域.无规卷曲是其二级结构中最大量的结构元件,α螺旋和延抻链分散于整个蛋白质中,活性位点的分析表明,编码蛋白有6类活性位点.分析双峰驼凝乳酶原基因及其编码蛋白质的特征,能够为深入开展双峰驼凝乳酶的表达和凝乳特性研究提供理论依据.

关 键 词:双峰驼  凝乳酶原  克隆  生物信息学
收稿时间:2013-11-19

Bioinformatics analysis of prochymosin gene in camelus bactrianus
YANG Yi,PU Yan and ZHANG Fuchun. Bioinformatics analysis of prochymosin gene in camelus bactrianus[J]. Chinese Journal of Bioinformatics, 2014, 12(1): 18-26
Authors:YANG Yi  PU Yan  ZHANG Fuchun
Affiliation:Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, Xinjiang 830046, China;Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, Xinjiang 830046, China;Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi, Xinjiang 830046, China
Abstract:In this paper the research on camelus bactrianus prochymosin gene sequence was illustrated using Bioinformatics methods to analyze amino acid sequence homology, physical and chemical characters, conserved domains, subcellular localization ,signal peptide, transmembrane domain, hydrophilic/hydrophobic ,and secondary structure. The results showed that the length of camelus bactrianus prochymosin is 1 146bp, encoding a protein with 381 amino acids. This protein belongs to pepsin A superfamily , and is a stable hydrophilic protein most probably located in endoplasmic reticulum (membrane). It has a signal peptide of 16 amino acids and no transmembrane domain. In the secondary structure, random coil is the majority of structural elements, while s-helix and extended stretch distribute throughout the protein chain. The active site analysis showed there are six kinds of active sites in the prochymosin. Analysis of camelus bactrianus prochymosin genes and the characteristics of their encoded proteins provide a theoretical reference to study curd characteristics and expression conditions.
Keywords:camelus bactrianus  Prochymosin  Cloning  Bioinformatics
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