Talin-1 head(hereinafter referred to as TH)is the head structure of talin protein,which contains a four-point-one-protein/ezrin/radixin/moesin(FERM)domain.Its F1 domain contains an unstructured loop of 30 amino acids(...Talin-1 head(hereinafter referred to as TH)is the head structure of talin protein,which contains a four-point-one-protein/ezrin/radixin/moesin(FERM)domain.Its F1 domain contains an unstructured loop of 30 amino acids(139-168),which does not interact with other domains.Because TH doesn’t get the crystal structure and whether the unstructured loop has obvious influence on the TH secondary structure,therefore,the truncated talin-1 headΔ139-168(hereinafter referred to as THΔ)was constructed and its structure and the impact of stability after truncation were analyzed.Molecular biology and structural biology methods were used to construct prokaryotic expression vectors of TH and THΔ,explore and optimize the expression conditions of recombinants,and they were purified by affinity chromatography and FPLC gel filtration chromatography.Finally,a large number of stable,high-purity protein samples were prepared successfully.The physicochemical properties and structural stability of the proteins were investigated by dynamic light scattering and circular dichroism.The results showed that the THΔsecondary structure of the truncated body did not change significantly,the structural stability was enhanced and the resistance to guanidine hydrochloride and high temperature was stronger.展开更多
利用高速脉冲 X 光摄影技术.对偏心多点起爆定向战斗部进行了实验研究,测试了两点起爆夹角分别为45°、60°和90°时杆条的飞散初速和飞散方向,并与中心起爆战斗部进行了对比。实验结果表明,对于偏心起爆战斗部,两点起爆夹...利用高速脉冲 X 光摄影技术.对偏心多点起爆定向战斗部进行了实验研究,测试了两点起爆夹角分别为45°、60°和90°时杆条的飞散初速和飞散方向,并与中心起爆战斗部进行了对比。实验结果表明,对于偏心起爆战斗部,两点起爆夹角为60°时,在目标方向上杆条数量增益较大。展开更多
基金Supported by the Scientific Research Personnel of Northeast Agricultural University(518001)。
文摘Talin-1 head(hereinafter referred to as TH)is the head structure of talin protein,which contains a four-point-one-protein/ezrin/radixin/moesin(FERM)domain.Its F1 domain contains an unstructured loop of 30 amino acids(139-168),which does not interact with other domains.Because TH doesn’t get the crystal structure and whether the unstructured loop has obvious influence on the TH secondary structure,therefore,the truncated talin-1 headΔ139-168(hereinafter referred to as THΔ)was constructed and its structure and the impact of stability after truncation were analyzed.Molecular biology and structural biology methods were used to construct prokaryotic expression vectors of TH and THΔ,explore and optimize the expression conditions of recombinants,and they were purified by affinity chromatography and FPLC gel filtration chromatography.Finally,a large number of stable,high-purity protein samples were prepared successfully.The physicochemical properties and structural stability of the proteins were investigated by dynamic light scattering and circular dichroism.The results showed that the THΔsecondary structure of the truncated body did not change significantly,the structural stability was enhanced and the resistance to guanidine hydrochloride and high temperature was stronger.
