摘要
相关研究表明mRNA序列中GC含量、回文密度和二级结构对蛋白质折叠速率都有重要影响,为了研究mRNA三级结构是否对蛋白质折叠速率也存在重要影响,收集了具有实验折叠速率的蛋白质作为研究对象,对其中的每一个蛋白质,计算其相应mRNA三级结构中各种局部碱基对梯阶参量值,并分析了这些参量值与相应蛋白质折叠速率的相关性。将蛋白质按照二级结构分类,进一步研究各局部碱基对梯阶参量对二级结构类蛋白质折叠速率的影响。结果显示,mRNA三级结构局部碱基对梯阶参量值与蛋白质折叠速率呈现出不同程度的相关性。表明短轴滑移量(shift)、长轴滑移量(slide)、z轴滑移量(rise)和平面短轴转角(tilt)等是影响蛋白质折叠速率的有效因素,说明mRNA三级结构对蛋白质折叠速率有重要影响。
In light of the influences of GC content in mRNA,the palindrome density and secondary structure of mRNA on protein folding rates reported in related research,we initiated the research on the influences of the tertiary structure of mRNA on protein folding rate.To analyze the correlation of the local basepair step parameters of mRNA tertiary structure with the protein folding rates,we collected the measured value of folding rate of some proteins,predicted tertiary structure of the proteins’mRNA and calculated the parameters of local base-pair step accordingly.Further,the proteins were classified according to their secondary structural to study the correlation of the local base-pair step parameters with the protein folding rates.The results revealed that the local base-pair step parameters of mRNA tertiary structure correlated with the protein folding rates in different extent,indicative of the fact that the parameters,shift in short axis,slide in long axis,rise in z-axis and plane tilt in short axis,were all the effective factors influencing on protein folding rates.The research demonstrated that the mRNA tertiary structure had pivotal effect on protein folding rates.
作者
程永霞
李瑞芳
赵瑞峰
宋鑫伟
CHENG Yong-xia;LI Rui-fang;ZHAO Rui-feng;SONG Xin-wei(College of Physics and Electronic Information,Inner Mongolia Normal University,Hohhot 010022,China)
出处
《内蒙古师范大学学报(自然科学版)》
CAS
2022年第2期134-141,共8页
Journal of Inner Mongolia Normal University(Natural Science Edition)
基金
内蒙古自治区自然科学基金资助项目(2019MS03042)
内蒙古自治区高等学校科学技术研究资助项目(NJZY17043)
内蒙古师范大学科研创新基金资助项目(CXJJSS19112)。
关键词
mRNA三级结构
局部碱基对梯阶参量
平移参量
旋转参量
蛋白质折叠速率
mRNA tertiary structure
local base-pair step parameters
translation parameters
rotations parameters
protein folding rate