利用圆二色谱法研究突变体BFR分子稳定性  

Detect the Stability of BFR Nano Capsule via CD

作　　者：孙晓明 康永红[2] 李周儒 殷文江 董国凯 李姗姗 蒯锦霞 马静媛 蔡红星 

机构地区：[1]徐州医科大学法医学教研室,徐州221002 [2]徐州市公安局物证鉴定所,徐州221008

出　　处：《科学技术与工程》2017年第21期208-211,共4页Science Technology and Engineering

基　　金：徐州医科大学优秀人才科研启动基金(A53591505;A53591504);徐州市科技局重点课题(KC15SM047);江苏省教育厅课题(16KJB340002)资助

摘　　要：通过引入人为突变,研究BFR纳米蛋白分子的稳定性与其一级结构的关系,探索蛋白质序列与结构的关系。选择可能与BFR构象密切相关的氨基酸残基引入突变,经表达、纯化后,利用圆二色谱仪检测突变体蛋白分子的结构变化。结果关键部位氨基酸的突变可以引起BFR分子中α螺旋含量及熔链温度发生了显著的变化。说明某些氨基酸的改变会引起BFR分子整体结构与稳定性的变化,有可能影响甚至改变蛋白质分子的功能。To study the effects of single amio acid mutation on the stability of BFR molecule, and explore the relationship between the amino acid sequence and the structure of the whole nano capsule, the amino acids which might affect the conformation of BFR molecule were mutated artificially. Circular Dichroism was applied to collect the parameters of the molecule structure. Results is that four mutated proteins were produced and detected. The mutation changed the percentage of a-helix of the BFR molecules. It ’ s conclused that those amino acids are important for keeping the BFR molecule intact. The mutations could introduce changes to the structure of the molecule and thus change the feature and function of i t , which may help us understand the relationship between the amino acid sequence and the molecule structure and function better.

关 键 词：细菌铁蛋白 圆二色 突变 蛋白纯化 

分 类 号：Q816[生物学—生物工程]