Natural-abundance oxygen-17 magnetic relaxation in aqueous solutions of apolar amino acids and glycine peptides.
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概要
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The spin-lattice relaxation times, <I>T</I><SUB>1</SUB>, of H<SUB>2</SUB><SUP>17</SUP>O have been measured for the aqueous solutions of 11 apolar amino acids and 5 glycine peptides as a function of the concentration at 25°C. The coordination numbers, <I>n</I><SUB>h</SUB>, and the rotational correlation times, τ<SUB>c</SUB><SUP>h</SUP>, of water molecules around the amino acids and peptides were estimated and compared with that of pure water, τ<SUB>c</SUB><SUP>0</SUP>. The value of τ<SUB>c</SUB><SUP>h</SUP>⁄τ<SUB>c</SUB><SUP>0</SUP>=1.87 for norleucine is the largest, while those of τ<SUB>c</SUB><SUP>h</SUP>⁄τ<SUB>c</SUB><SUP>0</SUP> for glycine peptides are almost the same 1.2. The value of <I>n</I><SUB>h</SUB>(τ<SUB>c</SUB><SUP>h</SUP>⁄τ<SUB>c</SUB><SUP>0</SUP>−1) was defined as the dynamic hydration number (DHN). The DHN showed a good correlation with several physicochemical properties, such as the molecular weights, partial molar volumes, adiabatic compressibilities, heat capacities, <I>B</I>-coefficients of the activity coefficent, and limiting diffusion coefficients of amino acids and glycine peptides in aqueous solutions.
- 公益社団法人 日本化学会の論文
著者
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Uedaira Hisashi
Department Of Materials Chemistry Faculty Of Engineering Hosei University
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Ishimura Miyuki
Department of Polymer Science, Faculty of Science, Hokkaido University
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