CONFIGURATION OF RANDOM POLYPEPTIDE CHAINS .2. THEORY
CONFIGURATION OF RANDOM POLYPEPTIDE CHAINS .2. THEORY
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DOI：
10.1021/ja01091a003
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发表时间：
1965-01-01
影响因子：
15
通讯作者：
FLORY, PJ
中科院分区：
文献类型：
--
作者：
BRANT, DA;FLORY, PJ
讨论根据等式计算的（r2）0/np/p2的值表I最后一列的下一列中列出了2个参数。这些结果的误差约为±10%; Mv的估计值构成了最大的不确定性来源。四个不同系统的结果的相似性是惊人的。结果表明，在所研究的体系中，涉及侧链或溶剂的特异性相互作用对多肽无规卷曲的无扰尺寸影响很小，表Ⅰ所列的四种多肽均以大侧链为特征。它们已在水溶液，酚类和酸性溶剂中进行了研究。多肽未扰动尺寸对氨基酸侧链没有任何可测量的依赖性，这使人们对蛋白质中第一相邻侧链之间相互作用的重要性产生了怀疑。
DiscussionValues of (r2) 0/np/p2 calculated from eq. 2 are presented in the next to the last column of Table I. These results are subject to errors of about±10%; the estimates of Mv constitute the largest source of uncertainty. The similarity of results for the four di-verse systems is striking. It strongly suggests that spe-cific interactions involving side chains or solvents exert little influence on the unperturbed dimensions of the polypeptide random coil in the systems examined.The four polypeptides listed in Table I are character-ized by large side chains. They have been investigated in aqueous, phenolic, and acidic solvents. The ab-sence of any measurable dependence of the polypeptide unperturbed dimensions on the amino acid side chains casts doubt on the importance of interactions between first neighbor side chains in proteins.