K33位乙酰化修饰SUMO蛋白的化学合成

HFCAS OpenIR

	K33位乙酰化修饰SUMO蛋白的化学合成
其他题名	Chemical Synthesis of K33 Acetylated SUMO Protein
	2016-01-01
发表期刊	高等学校化学学报
ISSN	0251-0790
摘要	采用高温辅助固相合成技术及基于多肽酰肼的自然化学连接技术,高效获得了小泛素相关修饰物（SUMO）蛋白及33位赖氨酸（K33）乙酰化SUMO蛋白.聚丙烯酰胺凝胶电泳（SDS-PAGE）和圆二色光谱分析结果表明,与生物表达蛋白相比,化学合成蛋白具有较好的纯度和类似的二级结构.
其他摘要	Sumoylated protein was found to reduce the protein binding force with the SUMO-interaction motif（ SIM） of effector protein when K33 of SUMO was acetylated. To further study the structures and mechanism,a large amount of uniformity acetylated SUMO protein was greatly needed. In this work,SUMO protein and K33 acetylated SUMO protein was efficiently obtained using high temperature assisted solid-phase peptide synthesis（ SPPS） technology combined with peptide hydrazide ligation. SUMO and K33 acetylated SUMO was identified with corrected molecular weight by the SDS-PAGE. It was also confirmed that the chemically synthe-tic protein and biologically expressed SUMO2 own similar homogeneity and secondary structure by the CD analysis. These results provided a foundation for the follow-up study of K33 acetylated SUMO protein.
关键词	小泛素相关修饰物乙酰化高温辅助固相合成多肽酰肼自然化学连接
收录类别	CSCD
语种	中文
CSCD记录号	CSCD:5849594
引用统计
文献类型	期刊论文
条目标识符	http://ir.hfcas.ac.cn:8080/handle/334002/66896
专题	中国科学院合肥物质科学研究院
推荐引用方式 GB/T 7714	. K33位乙酰化修饰SUMO蛋白的化学合成[J]. 高等学校化学学报,2016,037.
APA	(2016).K33位乙酰化修饰SUMO蛋白的化学合成.高等学校化学学报,037.
MLA	"K33位乙酰化修饰SUMO蛋白的化学合成".高等学校化学学报 037(2016).