TRANSPORT OF SULFONYL UREA DERIVATIVES BY TIME RESOLVED FLUORESCENCE METHODS

我们正在研究的结构，平衡动力学， 人催乳素的折叠。 催乳素是199个残基的成员， 造血细胞因子家族，包括生长激素。 催乳素涉及大量的生化途径，但 因其在怀孕期间促进泌乳的作用而得名。 生长激素和生长激素结合的X射线结构 催乳素受体的细胞外结构域 造血激素作用的一般特征; 结构是一个四螺旋束，具有不寻常的上-上-下-下 拓扑结构，它的作用是诱导受体的二聚化， 两步顺序绑定过程。 生长激素结合到 体细胞受体和催乳受体。 与此相反， 催乳素仅与催乳素受体结合。 此外，锌是 已知介导生长激素的受体结合，而 似乎在催乳素结合中不起作用。 因此，催乳素 远未进行详细的结构分析，因此， 负责生长激素的行为差异， 催乳素仍然无法解释。 我们正在执行 催乳素溶液结构的高分辨多核 匪r 我们正在研究催乳素的折叠和稳定性 使用平衡离心、圆二色性、扫描 量热法和氢交换动力学。 ESI和NLkLDI质量 光谱法用于测定蛋白质分子量， 二硫键的位点。

We are investigating the structure, equilibrium dynamics, and folding of human prolactin. Prolactin is a 199-residue member of the hernatopoietic cytokine family, which includes growth hormone. Prolactin is implicated in a large number of biochemical pathways, but it is named for its role in promoting lactation during pregnancy. X-ray structures of growth hormone andgrowth hormone bound to the extracellular domain of the lactogenic receptor have given insights into the general features of hematopoietic hormone action; the native structure is a four-helix bundle with an unusual up-up-down-down topology, and it acts by inducing dimerization of thereceptor in a two-step sequential binding process. Growth hormone binds to both the somatogenic receptor and to the lactogenic receptor. In contrast, prolactin binds only to the lactogenic receptor. In addition, zinc is known to mediate receptor binding of growth hormone, whereas it does not appear to play a role in prolactin binding. Prolactin has thus far eluded detailed structural analysis, and so the molecular details responsible for the difference in the behavior of growth hormone and prolactin remain unexplained. We are carrying out the determination of the solution structure of prolactin by high resolution multinuclear NMR. We are investigating the folding and stability of prolactin using equilibrium centrifugation, circular dichroism, scanning calorimetry, and hydrogen exchange kinetics. ESI and NLkLDI mass spectrometry are used to determine the protein molecular weight and sites of disulfide linkage.