EIKEN嗜肺军团菌检测试剂盒

广州健仑生物科技有限公司

主要用途：用于检测尿样中嗜肺军团菌血清型1抗原，以支持军团菌感染的诊断。

产品规格：20T/盒

存储条件：2-30℃

EIKEN嗜肺军团菌检测试剂盒

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【产品介绍】

EIKEN

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【公司名称】 广州健仑生物科技有限公司
【】    杨永汉 
【】 
【腾讯 】 2042552662
【公司地址】 广州清华科技园创新基地番禺石楼镇创启路63号二期2幢101-3室
【企业文化】

研究人员表示，这项新发现明确了多种不同脑部疾病的共同机理，并为延缓那些已经表征痴呆症状的患者的治疗指明了道路。
膜蛋白对于光合作用、视觉等功能至关重要。它们还是细胞的看门人，能决定什么可能会通过细胞膜，也帮助从细胞膜外部输入养料和将内部垃圾输出。由于这些多重角色，它们构成了很大一部分的药物靶点。虽然它们的功能很明确，但是关于它们如何折叠的信息却远远落后于球状蛋白质。
Wolynes及其同事使用原始的基因组信息，来预测氨基酸链将如何通过遵循阻力zui小的途径(取决于链上每个残基相关的能量)，折叠成为功能蛋白质。一个蛋白质越接近于其功能性“原始”状态，它就会越稳定。Wolynes的开创性理论生动地将这种能量描绘成一个漏斗。
为了检测他们的计算机模型，研究人员将它们与X射线晶体学获得的真实蛋白质结构进行比较。大量的结构对球状折叠的蛋白质是可用的，这些蛋白漂浮在体内，执行生命*的任务。
但直到zui近几年，我们已经很难获得跨膜蛋白的相似结构，因为要提取它们用于成像，同时又不会破坏它们，难度非常的大。zui近有研究人员利用一种去垢剂洗掉目的蛋白上的大多数膜，Wolynes称：“它在蛋白质周围留下一个脂肪层，但是却给出一种涂层，可使整个分子在后来形成晶格。”
当Wolynes注意到，两种广泛使用的细胞生物学教材对于跨膜蛋白如何折叠有*不同的意见时，受到启发研究膜蛋白。他说：“其中一本教材，列出所有规则，说：‘这是证据表明，它是动力学控制的。’另外一本教材指出：‘这是证据表明，它是热力学控制的。’它们以那种方式被写入教材，好像是确定。我想说我仍然不确定，但我认为我们的工作更多地指出，折叠是热力学(平衡)控制的，至少一次蛋白质是停留在膜中。”
Kim和Schafer修改了Wolynes实验室使用的一种蛋白质折叠算法，被称为联想记忆、水介导的结构和能量模型(AWSEM)，来解释膜蛋白所*的外界影响，包括将部分折叠蛋白质插入膜的易位子机制和膜本身。
利用这种算法，他们成功地确定，热力学漏斗在膜蛋白折叠中似乎仍然占据上风，如同它们为球状蛋白质所做的。
Kim称：“我们有来自许多不同实验室的膜蛋白结构数据库，我们能了解在它们之间转换的参数。这些参数两个残基(珠)应该相互作用的多么强烈，并考虑周围的环境。这可让我们能够从原始序列做出预测。”

The researchers said the new findings pinpoint common causes of many different brain diseases and point the way to delaying the treatment of those who already have symptoms of dementia.
Membrane proteins are essential for photosynthesis, vision and other functions. They are also gatekeepers to cells that determine what may pass through the cell membrane and also help to input nourishment from the exterior of the cell membrane and to export internal junk. Due to these multiple roles, they constitute a large part of the drug target. Although their function is clear, the information about how they fold is far behind globular proteins.
Wolynes and colleagues use the raw genomic information to predict how amino acid chains will fold into functional proteins by following the pathway of least resistance (depending on the energy associated with each residue on the chain). The closer a protein is to its functional "primitive" state, the more stable it will be. Wolynes' pioneering theory vividly portrays this energy as a funnel.
To test their computer models, the researchers compared them to the actual protein structures obtained by X-ray crystallography. Numerous structures are available for globularly folded proteins that float in the body and perform essential tasks of life.
However, it has been very difficult to obtain similar structures of transmembrane proteins in recent years because it is extremely difficult to extract them for imaging without damaging them. Recently, researchers have used a detergent to wash away most of the membrane on the protein of interest, Wolynes said: "It leaves a layer of fat around the protein, but gives a coating that allows the entire molecule to form later Lattice. "
Wolynes was inspired to study membrane proteins when he noted that the two widely used textbooks on cell biology have compley different opinions about how the transmembrane proteins fold. He said: "One of the textbooks lists all the rules, saying: 'This is evidence that it is kinetically controlled.'" Another textbook states: 'This is evidence that it is thermodynamically controlled.' ' It seems to be absoluy certain that the text was written in that way, and I would like to say that I am still not sure, but I think our work more often states that the folding is thermodynamically (equilibrium) controlled, at least once the protein is stuck in the film "
Kim and Schafer modified a protein folding algorithm used by Wolynes Lab called associative memory, water-mediated structure and energy model (AWSEM) to account for the external effects unique to membrane proteins, including the insertion of partially folded proteins Membrane translocation mechanism and membrane itself.
Using this algorithm, they succeeded in determining that the thermodynamic funnels still seem to hold the upper hand in membrane protein folding as they do for globular proteins.
"We have a database of membrane protein structures from many different laboratories and we know the parameters that switch between them." These parameters specify how strongly two residues (beads) should interact and take into account the surrounding environment This allows us to make predictions from the original sequence. "