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构象变化的英文

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"构象变化"怎么读用"构象变化"造句

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  • comformational change
  • conformational change

例句与用法

  • Computer simulation techniques can be used to understand the properties of a molecular system in terms of interactions at the atomic level
    Md模拟通过给出生物大分子在原子水平上的相互作用,提供生物大分子的涨落和构象变化的详细信息。
  • In this paper , we consider more of the conformational changes in the process of atp ' s hydrolysis and the complex structure of microtubule
    基于这种情况,本论文进一步考虑了驱动蛋白在实际运动中,尤其是在atp水解为adp过程中的构象变化以及微管结构的复杂性。
  • In kinesin ' s actual movement , it continuously changes its conformation to catalyze atp ' s hydrolysis . the role of microtubule is not a simple periodic potential
    在实际运动中,马达不断进行着自身构象变化并催化atp水解,微管产生的势场也不仅仅是一个简单的周期势函数。
  • By exploiting recent technical advances , we are able to observe , detect , even manipulate individual molecules and study their conformational changes and dynamic behaviors
    近来,科学技术的探索发展使我们可以观察、检测甚至操纵单个分子并且研究它们的构象变化和动力学行为。
  • We can take molecular motor as a brownian particle in the case of ignoring the conformational changes . the interaction between motor and microtubule can be described by a special potential function and the effect of the environment can be simplified as a noise
    在不考虑分子马达构象变化的情况下,通常把分子马达抽象为布朗粒子,用一个特定的势函数来表示轨道与马达的相互作用,环境的影响可以简化为特定形式的噪声激励。
  • Abstract : the effects of terbium ion on the conformation of calmodulin and on the interaction between calmodulin and melittin have been studied by the endogenous fluorescent spectrometry of calmodulin and melittin , and the sensitized fluorescent spectrometry of terbium ion , respectively . the results show that terbium ions have a tight binding site in the i and ii metal - binding sites of calmodulin . the conformation of calmodulin induced by terbium ion can bind melittin and transfer the tryptophane residue of melittin to a relatively hydrophobic environment , while the binding of melittin to calmodulin produces effect on the binding orders of terbium ion in camodulin . results from ft - ir spectrometry have revealed that upon binding of lanthanum ion , apo - calmodulin undergoes a conformational change with the increase of - helix content and the decrease of - sheet content . melittin ' s binding to calmodulin has no effect on its conformation induced by the binding of lanthanum ion to calmodulin
    文摘:分别用钙调蛋白和蜂毒素的内源荧光光谱以及铽离子的敏化荧光光谱考察了铽离子对钙调蛋白构象变化以及对钙调蛋白与蜂毒素相互作用的影响.结果表明,铽离子首先结合在钙调蛋白的第和第位点,铽离子不影响钙调蛋白与蜂毒素的相互作用,蜂毒素与钙调蛋白作用后不影响铽离子在钙调蛋白上的键合顺序.傅里叶变换红外光谱结果表明三价的镧离子与钙调蛋白作用使钙调蛋白的螺旋结构增加,折叠结构减少,与钙离子对它的二级结构影响相类似.稀土离子在钙调蛋白-蜂毒素复合体系中主要与钙调蛋白作用
  • The results indicate that because of the improvement in two aspects mentioned above , the successful probability of the docking prediction is increased from unbound structures . for the case of enzyme trypsin - inhibitor appi , although the large conformational change occurs to the arg 15 side chain of appi upon complex formation , the native - like structure was still found and ranked first
    其中,在胰蛋白酶appi复合物结构预测中,尽管抑制剂appi的15号残基arg侧链在复合物形成过程中发生了较大的构象变化,但其近天然结构仍然被找到了,并在打分中排在了第一位。
  • Part i this paper has minutely studied the interaction between ag ( i ) and serum albumin . the binding of ag ( i ) to human serum albumin ( hsa ) or bovine serum albumin ( bsa ) has been studied by equilibrium dialysis at ph ( 5 . 4 ) . the scatchard analysis indicates that there exists several strong binding sites of ag ( i ) in both hsa and bsa . a notable hysteretic effect has been observed in the interaction of ag ( i ) with hsa or bsa using uv - visible spectrometry at ph ( 5 . 4 ) , which shows that the binding between ag ( i ) with hsa or bsa may induce a slow transition of hsa or bsa from the conformation of weaker affinity for ag ( i ) to one of stronger affinity ( a - b transition ) . the rate constants and activation parameters of this transition parameters of this tansition were measured and discussed . the binding equilibrium has been also studied by resonance light - scattering spectrum ( rls ) and flurescence quenching
    第一部分:等离子点ph ( 5 . 4 )条件下,用平衡透析法和紫外光谱,荧光光谱,共振散射光谱研究了ag ( )与人血清白蛋白( humanserumalbumin ,简称hsa )或牛血清白蛋白( bovineserumalbumin ,简称bsa )的结合。 scatchard图分析表明, ag ( )在hsa或bsa中有强弱两类结合部位,通过计算机拟合获得结合的逐级稳定常数值。紫外扫描发现ag ( )与hsa或bsa的结合存在滞后效应,表明ag ( )与hsa或bsa的结合可能诱导蛋白质构象发生缓慢变化( a - b ) ,测得并讨论了这一构象变化的速度常数和活化参数。
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