哪位高人也帮我找篇论文翻译 关于化学的 最好跟甘氨酸有关的 截取2000字左右就行 谢谢了！急用啊！ 求一篇关于中学化学教育的英文文献和中文翻译。。。 大概200...
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Chemistry is a very important subject. It is of as great importance as mathematics and physics. However, chemistry is also very difficult to learn. How to study chemistry is a big problem for high school students. However, I have some tips for you high school students, which you may find useful.
Tip number one. Chemistry is a little similar to English. As you all know, English sentences consist of words, and words consist of twenty-six letters and letter combinations. In "You and Me online English course", there are some tips of how to learn the twenty-six letters and the letter combinations, words and sentences. In chemistry, similarly, you should memorize the elemental symbols, chemical formulae and chemical equations. The chemical equations are similar to English sentences and the chemical formulae are similar to words. The elemental symbols are similar to letters. These are the basic things you need to memorize.
Tip number two. You should do the experiments closely. When you do them, you should look at the status of the reactants, the phenomena that happen in the chemical reaction, the conditions of the reaction and the color and state of the resultants . For example, when magnesium burns, it produces a lot of heat and gives white dazzling light, and becomes a white substance called magnesium oxide. Its chemical equation goes like this: 2Mg+O2=2MgO(lit). It is a chemical change because in the change, a new substance has been formed.
Tip number three. You should review after you learned a unit or two of the textbook, or they will become easy to forget. Some knowledge are really confusing for us students, so you should distinguish one piece of knowledge from another.
Tip number four. The fourth tip that I would give you high school students is error correcting. Don't believe that what is in your textbook is always correct. Nope. When I was a high school student, I used a new set of chemistry textbooks. The chemistry textbooks has a lot of errors and some of the important knowledge and chemical equations has been deleted from the book. So some of the chemical equations are nowhere to be found in the book. For example, the chemical reactions of making hydrogen sulfide and sulfur dioxide in the lab, or the oxydizability of nitric acid, have been deleted from the textbook, so I had to look up my old chemistry book, which a lot of people used for going over their lessons in 1977. That is a good idea for you, too. If your textbook has an error, you should correct the error. If the important knowledge has been deleted from the book, you also should add it to the textbook.
If you follow my tips, you will surely learn chemistry well.
A, GlyR distribution in the CNS
glyR in the spinal cord and medulla oblongata in a high level of expression, and in the midbrain, hypothalamus and thalamus in the lower brain areas are not high-level expression. This distribution pattern of GlyR and Gly in the spinal cord and brain stem as the major inhibitory neurotransmitter in line to play a role. It is interesting to note, GlyR and GABAAR often co-exist in the spinal cord neurons [2], suggesting that Gly and GABA transmitters may be used as a total (cotransmitter), in the spinal cord play a total transfer (cotransmission) role [3,4].
From the adult rat spinal cord GlyR purified by the α1 and β subunits of the different polymer components, roughly in the ratio of α1: β = 3:2. In contrast, there is evidence that the embryos of five GlyR is composed of α2 subunit with the dimer. Α2 in vitro with the reorganization of polymer and the functional characteristics of embryonic GlyR is also very consistent. In addition, the spinal cord in rats found only low levels of α3 mRNA, prompted α3 may be accounted for in the proportion of GlyR smaller. β subunit is not easy to form a separate polymer with GlyR, but effectively with α1, α2 or α3 different polymer combination. On the other hand, even in the absence of β subunit, α1, α2 and α3 form a reorganization can also GlyR.
α1 subunit mRNA distribution and adult spinal cord and brain stem in the 3H-strychnine binding site is similar to. However, it was surprising that the β subunit to the high number of mRNA in the adult CNS in a whole. The existence of high-level brain regions β subunit mRNA and some people difficult to understand, because the β subunit can not form a separate function of GlyR. GlyR subunit intracellular gephyrin more extensive distribution of mRNA in the rat CNS expression in all regions. Although GlyR in adult animals, almost lack of higher brain areas such as, but in the acute separation and primary culture of neonatal rat hippocampal neurons have been observed by the Gly-induced current response. Recently, Flint, etc. [5] reported that during the early development of rat neocortex, non-synaptic release of taurine can activate GlyR area. Embryonic period as a result of taurine can lead to deprivation of cortical dysplasia. That taurine may therefore activate non-synaptic GlyR affected parts of the development of neocortex.
In the sub-cellular level, GlyR to "cluster" approach in the cell surface. It is assumed in the cell body and dendrites of the "cluster" is located on the synaptic connections. In the process of cell culture, gephyrin to the GlyR cluster is necessary, gephyrin can be anchored receptor on the cell cytoskeleton. In addition, recent studies have shown that early in embryonic development, the activation of excitatory GlyR not have inhibitory effects [6,7], GlyR a "cluster" is due to glycine receptor activation caused by voltage-dependent Ca2 + channel openers, and the resulting influx of Ca2 + regulation [7].
Second, GlyR molecular structure
(A) the structure of GlyRα subunit and β subunit each from the 420 and 470 amino acid residues (figure). By hydrophobicity analysis, forecasts GlyR subunit with a long extracellular N-terminal area, four transmembrane domain (referred to as M1-M4) and a home between the M3-M4 loop of the large cells. This is the general model structure LGICs. N-terminal of the GlyR contains at least one potential N-glycosylation sites (such as α1 first 38 residues N), this area is likely to exist two pairs of sulfur chain. Central is the first Cys-138 and Cys-152 (α1 subunit counting), through disulfide bond formation, the ring is at all conservative LGICs; M1 second ring around the district, is Cys-198 and the formation of Cys-209. In the α and β subunit M3 and M4 cells between the inner ring large initial Department, there are some positively charged residues and contains protein kinase phosphorylation sequence.
(B) receptor assembly and expression has been proved to be the impact of several amino acid residues of recombinant α-subunit assembly. First of all, N38A will enable the replacement of Gly-activated currents had disappeared and could not form N38A glyR note that the α-subunit only in the form of assembly glycosylation. Secondly, the Cys-138 and / or Cys-152 mutation of Ser and / or Ala, its chain disulfide solution, the same can not function in the formation of GlyR, that receptor assembly is impeded. Ring to replace other residues can also produce similar results. For example, Ala, or Asn in place of Asp-148 to enable the expression of GlyR blocked. Although replaced by the more conservative D148E produced by wild-type GlyR and GlyR have similar features, but the mutant receptor on the sensitivity of strychnine reduced. In view of this, the first loop of the receptor LGICs assembly is required. The second ring may have the same effect. Because Cys-198 replaced by Ser (C198S) hinder the assembly of GlyR; with a short-chain residues of the replacement ring when Tyr-202 have the same consequences. At the same time as a result of Tyr-202 is also an important ligand binding residues (see below), the latter found to have attention. Strangely enough, when Cys is replaced by Ser (C209S) when, α1 subunit can be assembled in the cell surface, but not strychnine or a combination of non-Gly-activated currents. The function of the second ring will also be discussed below. In addition, the M2 subunit α1 domain to Asn, Gln or Glu alternative edge of cells has hampered the Arg-252 receptor assembly.
Although early in development or in vitro use of recombinant α technologies used to produce polymer with the same adult α / β dimer different pharmacological characteristics similar, but the α and β subunit co-expression can greatly enhance the efficiency of receptor assembly. β subunit may be some with the α-subunit interaction mechanism to influence the assembly of receptors.-------------下面是上面英语的翻译-----------------------------------
甘氨酸受体(GlyR)介导的抑制性神经传递在哺乳动物中枢神经系统(CNS)反射活动、随意运动调节和感觉信号的处理中具有重要作用〔1〕。GlyR五聚体由三个独立的多肽组成：两个糖蛋白(48 kD和58 kD)，分别称为α和β亚单位，另一个为93 kD的细胞质蛋白，叫“gephyrin”。GlyR与尼古丁型乙酰胆碱受体(nAChR)、GABAA受体(GABAAR)、5-HT3受体(5-HT3R)等具有很大的同源性。它们一起形成一个配体门控离子通道（LGICs）超家族。LGICs的五个跨膜亚单位形成离子通道孔区。就GlyR而言，该离子通道选择性地通透Cl-。
一、GlyR在CNS中的分布
glyR在脊髓和延髓中以高水平表达，而在中脑、下丘脑和丘脑中较少，高级脑区则不表达。GlyR的这种分布模式与Gly在脊髓和脑干中作为主要的抑制性神经递质发挥作用是一致的。有趣的是，GlyR和GABAAR常常共存于脊髓神经元中〔2〕，提示Gly和GABA可能作为共递质(cotransmitter)，在脊髓内发挥共传递(cotransmission)作用〔3，4〕。
从成年大鼠脊髓中纯化的GlyR是由α1和β亚单位组成的异聚体，其比例约为α1∶β=3∶2。相反，有证据表明胚胎GlyR是由五个α2亚单位组成的同聚体。体外重组的α2同聚体与胚胎GlyR的功能特性也十分一致。另外，在大鼠脊髓中仅发现低水平的α3 mRNA，提示α3在GlyR中可能占比例较小。β亚单位单独不易形成同聚体GlyR，但能有效地与α1、α2或α3结合形成异聚体。另一方面，即使没有β亚单位，α1、α2和α3也可以形成重组GlyR。
α1亚单位mRNA的分布与成体脊髓和脑干中3H-士的宁结合位点相似。但令人惊奇的是β亚单位mRNA以很高的数量出现在成体整体CNS中。高级脑区存在β亚单位mRNA有些让人难以理解，因为β亚单位单独不能形成有功能的GlyR。GlyR细胞内gephyrin亚单位mRNA的分布更加广泛，在大鼠CNS所有区域都有表达。尽管GlyR在成体动物的高级脑区几乎缺如，但在急性分离的和原代培养的新生大鼠海马神经元上，均已观察到由Gly诱导的电流反应。最近，Flint等〔5〕报道，在大鼠新皮质发育早期，非突触释放的牛磺酸可使该区的GlyR激活。由于胚胎期牛磺酸剥夺能引起皮质发育不全。因此推测牛磺酸可能通过激活非突触部位GlyR影响新皮质的发育。
在亚细胞水平，GlyR以“簇”的方式分布在细胞的表面。据推测出现在胞体和树突上的“簇”位于突触连接点上。在细胞培养过程中，gephyrin对GlyR的簇集是必需的，gephyrin可以将受体锚定于细胞骨架上。此外，最近有研究表明，在胚胎发育早期，激活GlyR产生兴奋性而非抑制性效应〔6，7〕，GlyR的“簇集”受到因激活甘氨酸受体而引起的电压依赖性Ca2+通道开放和由此产生的Ca2+内流的调节〔7〕。
二、GlyR的分子结构
(一)亚单位结构 GlyRα和β亚单位各由420和470氨基酸残基组成(附图)。经疏水性分析，预测GlyR亚单位含一个长的N-末端细胞外区，四个跨膜结构域（称为M1-M4)和一个居M3-M4之间的大的细胞内环。这是所有LGICs结构的普遍模式。GlyR的N-末端含有至少一个潜在的N-糖基化位点(例如α1的第38位残基N)，此区域很可能存在两个双硫链环。第一个环是由Cys-138和Cys-152(α1亚单位记数）通过二硫键形成的，该环在所有LGICs中是保守的；第二个环靠近M1区，是由Cys-198和Cys-209形成的。在α和β亚单位M3和M4之间大的细胞内环起始部，有一些带正电荷的残基并包含蛋白激酶磷酸化序列。
(二)受体组装和表达 业已证明有几个氨基酸残基影响重组α亚单位的组装。首先，N38A替换可使原先Gly激活的电流消失，说明N38A glyR无法形成，即α亚单位只能以糖基化形式组装。其次，将Cys-138或/和Cys-152突变为Ser或/和Ala，使其二硫键解链，同样不能形成有功能的GlyR，推测是阻碍了受体组装。替换环内其它残基也可产生相似的结果。例如，用Ala或Asn代替Asp-148使GlyR表达受阻。尽管较保守地替换成D148E产生的GlyR与野生型GlyR有相似的功能特性，但突变受体对士的宁的敏感性降低。由此看来，第一个环对LGICs受体的组装是必需的。第二个环可能有同样的作用。因为将Cys-198替换为Ser（C198S）阻碍GlyR组装；用一个短链残基置换环内的Tyr-202时也产生同样后果。由于Tyr-202同时还是一个重要的配体结合残基(见下文)，后一发现已引起重视。奇怪的是，当Cys替换为Ser（C209S）时，α1亚单位虽然可以在细胞表面组装，但不能结合士的宁或不产生Gly激活电流。第二个环的功能还将在下文中讨论。此外，在α1亚单位的M2结构域，以Asn、Gln或Glu替代细胞内边缘的Arg-252也防碍受体组装。
尽管在发育早期或在体外运用重组技术产生的α同聚体具有与成体α/β异聚体相近的药理学特性，但是α和β亚单位的共表达可以大大地提高受体组装的效率。β亚单位可能是通过某种与α亚单位的相互作用的机制来影响受体的组装的。
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