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Solid-state proton relaxation and molecular motion in amino acids

机译:固态质子弛豫和氨基酸分子运动

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摘要

A proton magnetic relaxation study has been carried out on a series of amino acids in the solid state in the temperature range 270 to 400 K. These amino acids displayed proton relaxation minima that could be explained due to the reorientation of either the NH_3 group or CH_3 group or both. The relaxation minima at lower temperatures are attributed to the reorientation of the CH_3 groups, while those at higher temperatures are attributed to reorientation of the NH_3 groups in the zwitter-ion form of the molecules. Relaxation constants, activation energies and time factors for all amino acids are determined.
机译:在270至400 K的温度范围内,对固态的一系列氨基酸进行了质子磁弛豫研究。这些氨基酸显示出质子弛豫最小值,这可以通过NH_3基团或CH_3的重新取向来解释。组或两者兼而有之。较低温度下的弛豫最小值归因于CH_3基团的重新取向,而较高温度下的弛豫最小值归因于分子的两性离子形式的NH_3基团的取向。确定所有氨基酸的弛豫常数,活化能和时间因子。

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