螺旋多肽链结构的弹性模量
Elastic Moduli of Helical Polypeptide Chain Structures.
作者信息
Enomoto S, Krimm S
出版信息
Biophys J. 1962 Jul;2(4):317-26. doi: 10.1016/s0006-3495(62)86857-x.
Abstract
The elastic moduli of the alpha-helix, polyglycine II, and the parallel-chain and antiparallel-chain pleated sheet structures have been calculated. A Urey-Bradley type of potential was used, extended by the inclusion of hydrogen bond stretching terms where appropriate. In the one instance where a valid comparison with experimental data can be made, viz, alpha-keratin, the calculations indicate that the matrix component, rather than being amorphous, probably contains an ordered structure of higher modulus than the alpha-helix.
摘要
已计算出α-螺旋、聚甘氨酸II以及平行链和反平行链褶皱片层结构的弹性模量。使用了一种Urey-Bradley型势，并在适当情况下通过纳入氢键拉伸项进行了扩展。在一个可以与实验数据进行有效比较的实例中，即α-角蛋白，计算结果表明，基质成分可能并非无定形，而是包含一种模量高于α-螺旋的有序结构。
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