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Enzyme hydration, activity and flexibility: A neutron scattering approach

机译:酶的水合作用,活性和灵活性:中子散射法

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摘要

Recent measurements have demonstrated enzyme activity at hydrations as low as 3%. The question of whether the hydration-induced enzyme flexibility is important for activity is addressed by performing picosecond dynamic neutron scattering experiments on pig liver esterase powders at various temperatures as well as solutions. At all temperatures and hydrations investigated here, significant quasielastic scattering intensity is found in the protein, indicating the presence of anharmonic, diffusive motion. As the hydration increases a temperature-dependent dynamical transition appears and strengthens involving additional diffusive motion. At low temperature, increasing hydration resulted in lower flexibility of the enzyme. At higher temperatures, systems containing sufficient number of water molecules interacting with the protein exhibit increased flexibility. The implication of these results is that, although the additional hydration-induced diffusive motion and flexibility at high temperatures in the enzyme detected here may be related to increased activity, they are not required for the enzyme to function. (c) 2006 Elsevier B.V. All rights reserved.
机译:最近的测量表明水合时酶的活性低至3%。水合诱导的酶的柔韧性对于活性是否重要的​​问题,可以通过在各种温度和溶液下对猪肝酯酶粉末进行皮秒动态中子散射实验来解决。在这里研究的所有温度和水合作用下,蛋白质中均会发现明显的准弹性散射强度,表明存在非谐,扩散运动。随着水合作用的增加,会出现并依赖于温度的动态跃迁,并伴随其他扩散运动而增强。在低温下,增加水合作用会降低酶的柔韧性。在更高的温度下,含有足够数量与蛋白质相互作用的水分子的系统显示出更高的柔韧性。这些结果的含义是,尽管此处检测到的酶在高温下额外的水合作用引起的扩散运动和柔韧性可能与活性增加有关,但酶发挥作用并不需要它们。 (c)2006 Elsevier B.V.保留所有权利。

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