CONFORMATIONAL-ANALYSIS AND HELICAL PREFERENCES OF NORMAL AND ALPHA,ALPHA-DIALKYL AMINO-ACIDS
CONFORMATIONAL-ANALYSIS AND HELICAL PREFERENCES OF NORMAL AND ALPHA,ALPHA-DIALKYL AMINO-ACIDS
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DOI：
10.1002/bip.360300506
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发表时间：
1990-01-01
期刊：
影响因子：
2.9
通讯作者：
MARSHALL, GR
中科院分区：
文献类型：
--
作者：
HODGKIN, EE;CLARK, JD;MARSHALL, GR
已经对L-丙氨酸和α-丙氨酸的右手螺旋结构进行了能量计算。甲基丙氨酸寡聚体。一种新的“3.610”-螺旋被描述为α-甲基丙氨酸肽。α，310和3.610结构形式对螺旋长度、介电常数和力场的影响进行了研究。势能面的相互转换的螺旋已经产生。在α中的310-螺旋甲基丙氨酸低聚物表现出一定程度的结晶和熵稳定性，这在丙氨酸中没有观察到。电压敏感离子通道的形成的结果的相关性进行了讨论。
Energy calculations have been performed on right-handed helical structures of L-alanine and .alpha.-methylalanine oligmers. A new ''3.610''-helix is described for .alpha.-methylalanine peptides. The dependence of the relative stability of the .alpha., 310, and 3.610 structural forms on helix length, dielectric, and force-field, in the gas phase, has been studied. Potential energy surfaces for the interconversion of helices have been generated. The 310-helix in .alpha.-methylalanine oligomers exhibits a degree of enthalpic and entropic stabilization not observed for alanine. The relevance of the results to the formation of voltage-sensitive ion channels is discussed.