AMP激活蛋白激酶（AMPK）包括一个催化亚基α和两个非催化亚基，β和γ。每个亚基又有不同亚型，组成1:1:1的三聚体复合物。在哺乳动物中，AMPK的活性是由细胞内AMP/ATP水平调控。AMP/ATP比值上升，AMPK活性提高，调节下游复杂的代谢通路，刺激ATP生成，抑制ATP消耗，所以AMPK被称为真核生物中细胞内的能量感受器。因为AMPK可能成为治疗肥胖症、二型糖尿病和其他相关代谢性疾病的药物靶点，所以针对AMPK活性调节机制的研究显得尤为重要。本实验将哺乳动物AMPK和植物SnRK1的功能性结构域的蛋白片段构建到真核表达载体中获得重组质粒，再将其转入大肠杆菌表达系统中诱导表达目的蛋白，经提纯浓缩获得高品质的蛋白质以用于后续实验。进一步的研究计划将主要集中在不同功能结构域蛋白的相互作用。

AMP-activated protein kinase (AMPK)，consists of a catalytic α subunit and two non-catalytic subunits, β and γ, each with multiple isoforms that form active 1:1:1 heterotrimers. In mammals, the activity of AMPK is regulated by celluar AMP/ATP levels. The increase of AMP/ATP ratio elevates the activity of AMPK to regulate multiple downstream targets, stimulating ATP production and inhibiting ATP consumption, so AMPK is a sensor of cellular energy status in eukaryotes. As AMPK may be a key drug target for obesity, type 2 diabetes and other related metabolic diseases, research on the regulatory mechanism of AMPK activity is very important. Sevreal protein fragments derived from functional domains of mammalian AMPK and plant SnRK1 were cloned into prokaryotic expression vector to gain recombined plasmids, which were transformed into E. coli expression system to be induced to expression target proteins with different tags. According to tags and properties, target peoteins were puried and concentrated to be of good quality for the following experiments. Further experiment directions will be focused on the protein interactions between different functional domains.