Molecular Motions of Polymers Having Helical Conformation. II. Poly-β-methyl-L-aspartate, Poly-β-benzyl-L-aspartate and Po1y-γ-benzyl-L-glutamate.
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概要
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Molecular motion in three synthetic polypeptides has been examined by proton magnetic resonance methods in the temperature range 90°-430°K. The observed temperature dependence of the NMR second moment has been accounted for in terms of the motion of the side chain substituent. It becomes evident that at 90°K poly-β-benzyl-L-aspartate and poly-γ-benzyl-L-glutamate are in the rigid lattice while for poly-β-methyl-L-aspartate side chain methyl group undergoes rotation. It is concluded that the helix of the polypeptides undergoes neither rotation nor oscinatjonina11temp6raturerangestudied.Theimmobilityofthehelixoftl]epolypeptidesisinterpretedintermsoftheexistenceofthesidechainsubstituentandtheintramo-ecularhydrogenbond.
- 社団法人日本物理学会の論文
- 1964-11-05
著者
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Hikichi Kunio
Department Of Polymer Science Faculty Of Science Hokkaido University
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Hikichi Kunio
Department Of Physics Faculty Of Science Hokkaido University
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