1.dehydroquinate dehydratase was a(α2/β2)3 peptide,of which a pair of anti-parallel β-strands existed in the N-terminus and a loop in the C-terminus;
脱氢奎尼酸酶结构域为(α2β2)3多肽,在N-端有一对反平行的β链,在C-端有loop环;
2.CEMA consists of eight amino acid from N-terminus of cecropin A and C-terminus of modified melittin. It maintains potent antibacterial activity and deprives of the hemolytic activity.
CEMA为人工合成的阳离子抗菌肽，由cecropinA的N-末端8个氨基酸残基和经改造的蜂毒素C-末端组成，既保持了很强的抑菌活性，又降低了溶血毒性。
3.Bsg6 protein contains a BTB(Broad-complex,Tramtrack,and Bric-a-brac) motif on the N terminus and two consecutive C_2H_2 zinc finger motifs on the C terminus.
Bsg6蛋白含有一个N端BTB(Broad-complex,Tramtrack,andBric-a-brac)结构域和两个C端C2H2型锌指结构域.
4.The C terminus of NP contains the type-specific B cell epitopes, which occupies C terminus, about half of NP.
上述研究结果提示，体外表达NP蛋白的高变区，有可能用于汉坦病毒的分型检测研究。
5.The cellular location and topology of 7a were determined by immunocytochemistry and we found that 7a protein was located at Golgi, with its N-terminus facing the cytoplasm and its C-terminus facing Golgi matrix.
我们用免疫细胞化学方法对7a的细胞内定位及拓扑异构性进行研究，发现其定位于高尔基体，N端朝胞浆，C端朝内腔。 同时我们在实验中注意到转染了7a的HEK293细胞与空细胞相比，增殖变得缓慢，推测其可能有增殖抑制作用。
6.Amino acid sequence analysis showed that there were abundant acidic and hydrophobic amino acid residuals at the 23th to 47th sites and the 111th to 126th sites in N-terminus side of SpltMNPV IE0,a typical double zinc-finger structure at 225th to 271th sites in C-terminus side,which was conservative in IE0 of the nine comparative insect baculoviruses.
氨基酸序列分析显示,在SpltMNPV IE0蛋白N-端23～47位以及111～126位富含酸性氨基酸和疏水性氨基酸残基,C′端第225～271位具有典型的CX2CX14CCX4CX2CX15CX2C双锌指基序,该结构在所比较的9个昆虫杆状病毒IE0蛋白中是十分保守的。
7.GST pull down assay and immunofluorescence assays showed that LIM domain 2 at the C-terminus of hhLIM is critical for its interaction with actin. The mutant of the LIM domain 2 in which two important Cys are replaced by Ser lost the capacity of hhLIM to interact with actin. Mutation of the LIM domain 1 at the N-terminus of hhLIM impaired the capacity of hhLIM to interact with actin.
GST-pull down和hhLIM及其突变体与actin细胞定位关系的免疫荧光分析结果表明,C端的LIM结构域2是hhLIM与actin结合所必需的,该结构域中的两个Cys置换为Ser后可使hhLIM结合actin的功能完全丧失,N端的LIM结构域1突变使hhLIM结合actin的能力下降.
8.Methods Three peptides were synthesized, which were the minimal CTL epitope peptide OVA_ 257-264 , OVA_ 257-264 -KDEL (with an ER retrieval signal Lys-Asp-Glu-Leu sequence at the carboxyl-terminus of OVA_ 257-264 ), and OVA_ 257-268 (with four naturally extended residues TEWT at the carboxyl terminus of OVA_ 257-264 ).
方法应用多肽固相合成技术将哺乳动物内质网滞留信号——赖氨酸-天冬氨酸-谷氨酸-亮氨酸(Lys-Asp-Glu-Leu,KDEL)基序融合在H-2Kb限制性CTL表位OVA257-264的羧基端,同时合成该表位和氨基端自然延伸四个氨基酸(TEWT)的对照肽OVA257-268。
9.DOC-2 has a phosphotyrosine interactingdomain (PID) on in its N-terminus and multiple proline-rich SH3 binding motifs in its C- terminus.
在其氨基端含有磷酸酪氨酸作用结构域(phosphotyrosine interactingdomain，PID／PTB domain)，羧基端含有多个富含脯氨酸的SH3结合区。
10.Methods:Plasmids pEZ1 (Wt PgFtsZ), pYW1(ZΔC01, missing 73 residues from the C-terminus of PgFtsZ) and pYW2 (ZΔC02, missing 128 residues from the C-terminus of PgFtsZ) were introduced into Escherichia coli BL21(DE3)pLysS to express and purify the purpose proteins.
方法 :将质粒 pEZ1(WtPgFt sZ ,野生型PgFtsZ)、pYW 1(ZΔC0 1,PgFtsZ的C末端缺失 73个氨基酸残基的变异型 )和pYW 2 (ZΔC0 2 ,PgFtsZ的C末端缺失 12 8个氨基酸残基的变异型 ,已去除了PgFtsZ的C末端非保守性的区域 )导入EscherichiacoliBL2 1(DE3)pLysS中表达 ,然后进行分离和纯化这些目的蛋白。
