H2O和D2O与免疫球蛋白G竞争缔合的低温~ 1H NMR研究
A Low-temperature 1H NMR Study of H2O and D2O Associated Competitively with Immunoglobulin G in Solution
摘要：
本文提出了一种利用低温1H NMR技术测定H2O-D2 O混合蛋白质溶液中不冻水的方法，来表征D2 O的竞争缔合作用，并研究免疫球蛋白G吸附的水化水的不均一性。直接数据的数量的氘吸附的免疫球蛋白G和等温线的水（D2 O）吸附的蛋白质溶液水合条件下获得。使用该方法简单地证实了D2 O的优先结合以及低D2 O浓度的同位素效应。的等温线的形状，类似于多分子吸附，演示了在冷冻溶液中的温度降低时，结合到不同的蛋白质原子组的重水同位素的分数的相对变化。在-35 ° C下，连接到带电和极性原子基团的主要部分似乎相关为2/3。吸附曲线表明，蛋白质粉中的非冻结水与界面水有直接关系。
英文摘要：
An approach has been proposed to characterize the competitive association of D2O and to study the heterogeneity of hydration water adsorbed by the protein, immunoglobulin G, using methodology for determining of non-freezing water in mixed H2O-D2O protein solutions by low-temperature 1H NMR technique. Direct data on the numbers of deuteriums adsorbed by immunoglobulin G and isothermals of water (D2O) sorption by the protein for solution hydration conditions were obtained. The preferential binding of D2O as well as the isotopic effect of low D2O concentrations was simply confirmed using this method. The shape of the isothermals, similar to that for polymolecular adsorption, demonstrates relative changes in the fractions of heavy water isotope bound to different groups of protein atoms on decreasing temperature in frozen solution. At -35 deg C the major fractions attached to charged and polar atomic groups appear to be related as 2/3. The adsorption curves indicate the direct relationship of non-freezing water to interface water in protein powders.
机构、总结、中文摘要均由AI分析而来，可能存在错误，请以论文正文为准。
