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首页> 外文会议>Conference on Biological Quality and Precision Agriculture II, Nov 6-8, 2000, Boston, USA >HYDRATION AND STABILITY OF THE SOME GLOBULAR PROTEINS IN THE NON-POLAR MEDIUM IN THE PRESENCE OF PHOSPHATIDILHOLINE
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HYDRATION AND STABILITY OF THE SOME GLOBULAR PROTEINS IN THE NON-POLAR MEDIUM IN THE PRESENCE OF PHOSPHATIDILHOLINE

机译：磷脂酰胆碱存在下非极性介质中某些球蛋白的水合和稳定性

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摘要

Intention of present work is research the influence of non-polar medium and phosphatidilholine on stability of the macromolecules and hydration of cytohrom-C, tripsine and insulin by use of methods laser Raman and Infrared spectroscopy and isotope H/D exchange. It is shown, that the non-polar environment causes convertible changes of spatial pattern of macromolecules a protein degree of order of macromolecules as a result of which is increased. The presence of water at a system results in a converse effect. At interaction of phosphatidilcholin with the protondonors groups a protein will derivate complexes with a hydrogen bonds. Thereof quantity of aminoacidic oddments which are generatrix a polar circuit of a plaited layer is augmented. The outcomes of the analysis of bands of compound tone of water testify to presence in a system of three varieties of water clusters distinguished by frequencies of libration oscillations. It is suspected, that the hydrophobic environment can cause reduction of movability of molecules of water in different clusters.
机译：本工作的目的是通过激光拉曼光谱和红外光谱法以及同位素H / D交换的方法研究非极性介质和磷脂酰胆碱对大分子稳定性以及细胞色素C，雷帕霉素和胰岛素水合的影响。结果表明，非极性环境引起大分子空间模式的可转换变化，其结果是大分子的蛋白质数量级增加。系统中水的存在会产生相反的效果。在磷脂酰胆碱与质子基团相互作用时，蛋白质将衍生出具有氢键的复合物。从而增加了褶皱层的极性回路产生的氨基酸残基的数量。水的复合色调带的分析结果证明，存在着以释放振荡频率为特征的三种水簇形式的系统。怀疑疏水环境会导致不同簇中水分子的可移动性降低。

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