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英译汉(有关生物化学的资料)

  HIV-2 proteaseAgain, for facilitating comparison, the training set used in the h function method (Poorman et al。, 1991) for HTV-2 protease was used here。
   The set consists of 22 oligopeptides, with 21 octapeptides and one heptapeptide。 The values of Pi(X) (i = 1,2, 。 。 。,8) obtained through this training set are listed in Table VI。
   Based on these values, 10 000 octapeptides were generated by Monte Carlo sampling and they formed an expanded training set for HTV-2 protease。
   Based on the expanded training set, the 800 conditional probability values were derived。 For the same reason as stated above for HTV-1 protease, before substituting these data into equations (3), (6) or (8) to calculate n , the following procedure was taken。
   If a non-conditional probability equals zero, e。g。 Pi(A) = 0 (i = 1,2, 。 。 。,8), then it should be replaced by。If a conditional probability equals zero, e。
  g。 Pj(A│C) = 0 (j = 4 or 6), then it should be replaced by。The 10 000 octapeptides thus generated by Monte Carlo sampling and the 800 conditional probability values derived from HTV-2 protease are stored in the computer and they are also available upon request。
   With these data, one can calculate n from equation (3), (6) or (8) for any given octapeptide or heptapeptide。 Again, the amplifying factor f = 10" was taken in calculating II for HTV-2 protease。
   It remains to determine the value of threshold e for HTV-2 protease for which we used the same optimization procedure as described above for the HTV-1 protease。
   The 22 cleavable oligopeptides were taken from Table VII and the non-cleavable peptides were taken again from the sequence of hen egg lysozyme。
   Indeed, in this protein, no HTV-2 protease cleavage sites were detected even after complete denaturation (J。Hui, unpublished results)。
  The optimization process is illustrated through Table VIE, where we can see that the total number of correct predictions reaches a maximum value of 144 when e = 1。
  8, which was taken as the threshold for HIV-2 protease。 Using this value, we can calculate A via equation (5)。 The predicted results for the 22 oligopeptides in the HTV-2 protease training set are listed in Table VQ。
   The values of A are all > 0, meaning that all these oligopeptides can be cleaved by HTV-2 protease, implying that the 2 - 4 - 6 subsite-coupled model is fully selfconsistent within the cleavable training set。
   Also it can be seen from Table VQ that incorrect predictions were obtained for two of the 22 oligopeptides if the h function method was applied。
   For the 122 octapeptides taken from the sequence of hen egg lysozyme, they all were found to have negative values of A, meaning the current method is also fully self-consistent with the non-cleavable training set。
   The 52 oligopeptides, investigated recently by means of kinetic analysis (T6zser et al。, 1992), are listed in Table DC。
   This is an independent set of oligopeptides that is outside of the development set in Table VII and it can be used to test the extrapo。

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2006-12-11

0 0
     我是学文的,对于生物化学不了解,下面是我尝试的翻译,肯定有很多出入,希望对你略有帮助。 Again, for facilitating comparison, the training set used in the h function method (Poorman et al。
    , 1991) for HTV-2 protease was used here。 The set consists of 22 oligopeptides, with 21 octapeptides and one heptapeptide。
   The values of Pi(X) (i = 1,2, 。   。 。,8) obtained through this training set are listed in Table VI。
   再次,为便于比较, 此处采用的训练集是用在 为热硫化二蛋白酶的H函数法(Poorman等。 、 1991年)。该集包括22寡肽,有21八肽 一个七肽。  通过这个训练集获得的Pi(X) (i = 1,2, 。
   。 。,8)值 列在表格六当中。 Based on these values, 10 000 octapeptides were generated by Monte Carlo sampling and they formed an expanded training set for HTV-2 protease。
     Based on the expanded training set, the 800 conditional probability values were derived。
   以这些值为基础,由蒙特卡罗抽样产生出 10000八肽和他们形成了一个扩大热硫化二蛋白酶的训练集。   基于扩大的训练集,导出了800条件概率值。 For the same reason as stated above for HTV-1 protease, before substituting these data into equations (3), (6) or (8) to calculate n , the following procedure was taken。
     If a non-conditional probability equals zero, e。g。 Pi(A) = 0 (i = 1,2, 。 。 。,8), then it should be replaced by。
  If a conditional probability equals zero, e。  g。 Pj(A│C) = 0 (j = 4 or 6), then it should be replaced by。
   出于如上所述的同样热硫化-1蛋白酶的原因, 在把这些数据代入方程(3), (6)或(8)计算N时, 采取以下程序。 如果一个非条件概率为零,例如 Pi(A) = 0 (i = 1,2, 。
     。 。,8), 如果一个条件概率为零, 例如, Pj(A│C) = 0 (j = 4 or 6), 那么它应该被更换。 The 10 000 octapeptides thus generated by Monte Carlo sampling and the 800 conditional probability values derived from HTV-2 protease are stored in the computer and they are also available upon request。
     With these data, one can calculate n from equation (3), (6) or (8) for any given octapeptide or heptapeptide。
   Again, the amplifying factor f = 10" was taken in calculating for HTV-2 protease。   因而 由蒙特卡罗抽样产生的10000八肽和 的和从800热硫化二蛋白酶产生的条件概率值 被储存在电脑里,也可供供索阅。
   有了这些数据, 为任何特定八肽和七肽,人们可以从计算公式(3),(6)或(8)里来计算 N再次, 扩大因素发f=10是为热硫化二-2蛋白酶。  取自计算II 。 It remains to determine the value of threshold e for HTV-2 protease for which we used the same optimization procedure as described above for the HTV-1 protease。
     The 22 cleavable oligopeptides were taken from Table VII and the non-cleavable peptides were taken again from the sequence of hen egg lysozyme。
     Indeed, in this protein, no HTV-2 protease cleavage sites were detected even after complete denaturation (J。
  Hui, unpublished results)。   它任然持续决定热硫化二蛋白酶的极限值e。 正如上面就热硫化二蛋白酶的所述,为此我们使用同样的优化程序,22个裂开寡肽是取自表七, 非裂开肽是取自鸡蛋溶菌酶的顺序。
   的确, 在这个蛋白质里, 甚至在完成变性后,仍然没有探测到热硫化二蛋白酶裂开痕( i, 未发表成果)。   The optimization process is illustrated through Table VIE, where we can see that the total number of correct predictions reaches a maximum value of 144 when e = 1。
    8, which was taken as the threshold for HIV-2 protease。 Using this value, we can calculate A via equation (5)。
   The predicted results for the 22 oligopeptides in the HTV-2 protease training set are listed in Table VQ。
     The values of A are all > 0, meaning that all these oligopeptides can be cleaved by HTV-2 protease, implying that the 2 - 4 - 6 subsite-coupled model is fully selfconsistent within the cleavable training set。
     优化过程是通过表八表示的,在这里我们可以看到当e=8时, 正确的估计总数达到了144的最大值,它也是 HIV-2 蛋白酶的最低限度。我们运用这些值可以通过公式(5)计算出A。
  表就列出的是为 HTV-2蛋白酶的训练集 里的22寡肽的预测结果。A的 值都大零,这意味着所有这些寡肽能被热硫化二蛋白酶切分, 暗示着2-4-6分偶合模式在裂开训练集里是完全自成一致的。   Also it can be seen from Table VQ that incorrect predictions were obtained for two of the 22 oligopeptides if the h function method was applied。
     For the 122 octapeptides taken from the sequence of hen egg lysozyme, they all were found to have negative values of A, meaning the current method is also fully self-consistent with the non-cleavable training set。
     从表九还可以看出,如果运用h函数法,就22 寡肽中的两个,可以得到错误的预测。对从鸡蛋溶菌酶顺序中取出的122八肽来说,我们发现了A的负值, 这意味着目前的方法也自己完全符合非可裂开的训练集。
   The 52 oligopeptides, investigated recently by means of kinetic analysis , are listed in Table DC。
     This is an independent set of oligopeptides that is outside of the development set in Table VII and it can be used to test the extrapo 表格DC所列出的是最近通过动力的分析(T6zser et al。
    , 1992)方式进行调查的52寡肽。这是一套独立的寡肽集,它在表七的发展集的外面。 它可以用来测试额外 肽。

2006-12-11

61 0
    HIV-2蛋白酶 (爱滋病毒存活的重要酵素) -----用蒙特卡羅方法預?y化?W健的交?位置 在使用H函?捣椒ㄖ?Poorman et al。, 1991文獻中提到這??概念) 用到的化合物﹐同?颖挥玫?IV-2蛋白酶的?y?中。
   這??化合物含有22??低聚?分子﹐21??八?分子和1??七?分子。   ?倪@??化合物中得到的值Pi(X) (i = 1,2, 。 。 。,8)顯示在表VI中。
   以這些?抵?榛A﹐用蒙特卡羅方法可以產生10 000??八?分子﹐這?萤oHIV-2蛋白酶的分子結??就?U大了。 根?@???U大後的化合物分子結??﹐我??得到800???l件概(??率值。
    上面我??曾提到?y?HIV-1蛋白酶﹐和它同?拥脑颟o在把800???l件概(??率值放入方程式(3), (6) 或 (8) ?碛?算出 n之前﹐要先?過下述步驟。
   如果非?l件概率值=0﹐比如﹐ Pi(A) = 0 (i = 1,2, 。 。 。,8)﹐那麼這??非?l件概率值要改成___。   如果?l件概率值=0﹐比如﹐ Pj(A│C) = 0 (j = 4 or 6)﹐那麼這???l件概率值要改成___。
   這?萤o通過蒙特卡羅方法所得到的10 000 八?分子和800???l件概率值可以?Υ嬖谟?算?C中﹐今後隨?r調用。 我??可以根?o定的八?分子和七?分子的?的咯o通過方程式(3), (6) 或 (8)?算出n。
    放大?S??f = 10再一次地被用?碛?算II 。 現在剩下的就是?算HIV-2蛋白酶的臨界值﹐這和我??上面提到的HIV-1蛋白酶一?萤o使用同?拥??化程序。 ?谋砀馰II中我??拿出22??具有親和力(或有交?性﹐偶?性)的低聚?分子﹐然後再?牡扒迦诰?中取出非親和力的?分子。
     ??際上﹐即使在?過完全?性(化合物結??發生完全?化)之後﹐我??也?]有在這??蛋白質中發現HTV-2 protease中存在的交?結合點。(J。Hui的?文﹐??唇?發表)。
   這????化過程顯示在表格VIE中。?e = 1。8?r﹐我???倪@??表格中看到﹐正確預?y出的??凳亲畲笾?44﹐這???抵稻褪荋IV-2 protease(HIV-2蛋白酶)的臨界值。
    用這???抵旦o我??可以通過方程式(5)?算出A。 在22??低聚?分子的情?r下﹐我??得到的預?y結果顯示在表格VQ中。 所有的A>0﹐這說明在HTV-2 protease(HIV-2蛋白酶)這??化合物中﹐所有的低聚?分子都可以在交?結合點?被?嚅_。
    這也表明﹐在化?W健可以在交?結合點?被?嚅_的化合物中﹐2 - 4 - 6??位(不是第一位﹐不是1﹐是2)偶合模式是完全能?蜃晕蚁嗷ソ宦?﹐?亩纬赏暾末o相連的化?W健。
   ?谋砀馰Q中我??也可以看到﹐如果使用H函?旦o22??中的2??低聚?分子預?y發生錯誤。   ?摹扒迦诰?’分子排列中取出的122??八?分子中﹐它??都是A的?值。
  這意味着﹐我??現在所用的?y?方法﹐即使在化?W健不能?嚅_的化?W物中﹐它??-這些八?分子﹐同?邮悄?蜃晕蚁嗷ソ宦?的。 (我補充一下﹐相互交?的意思是指具有親和力﹐比如化?W物中的不同官能?F能?蚧ハ噙B接﹐?亩纬尚碌幕?W結??。
    這裡的?﹐??是月字偏旁﹐我的中文?件打不出?愆o是指含有氨基酸官能?F的分子) 通過分子?恿?W (T6zser et al。, 1992的?文中提到這??概念)分析﹐這52??低聚?分子結??顯示在表格DC中。
  這些低聚?分子是?立的﹐和表格 VII中顯示的低聚?分子不同﹐它??可以用??y?。  。。。(你的文章?]了。。) 。

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