α螺旋-线团相变：从头算理论预言的分析
Alpha helix-coil phase transition: analysis of ab initio theory predictions
摘要：
在本文中，我们提出的计算结果与使用的理论方法在我们的前一份文件[1]中所描述的，并进行详细的分析α螺旋-随机卷曲转变的丙氨酸多肽的不同长度。我们已经计算了多肽的势能面与它们的扭曲自由度，并使用建议的方法[1]构建了多肽的无参数配分函数。从建立的配分函数中，我们推导出不同长度的丙氨酸多肽的各种化学特性作为温度的函数。因此，我们分析了由21，30，40，50和100个氨基酸组成的丙氨酸多肽的热容，潜热和螺旋度的温度依赖性。另外，我们已经获得了相同的物理特性，从使用分子动力学模拟，并比较它们与新的统计力学方法的结果。比较证明了统计力学方法的有效性，并建立其准确性。
英文摘要：
In the present paper we present results of calculations obtained with the use of the theoretical method described in our preceding paper [1] and perform detail analysis of alpha helix-random coil transition in alanine polypeptides of different length. We have calculated the potential energy surfaces of polypeptides with respect to their twisting degrees of freedom and construct a parameter-free partition function of the polypeptide using the suggested method [1]. From the build up partition function we derive various thermodynamical characteristics for alanine polypeptides of different length as a function of temperature. Thus, we analyze the temperature dependence of the heat capacity, latent heat and helicity for alanine polypeptides consisting of 21, 30, 40, 50 and 100 amino acids. Alternatively, we have obtained same thermodynamical characteristics from the use of molecular dynamics simulations and compared them with the results of the new statistical mechanics approach. The comparison proves the validity of the statistical mechanic approach and establishes its accuracy.
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