Malkov Sasa N, Zivković Miodrag V, Beljanski Milos V, Stojanović Srdan D, Zarić Snezana D
Department of Mathematics, University of Belgrade, Studentski Trg 16, 11000, Belgrade, Serbia.
Protein J. 2009 Feb;28(2):74-86. doi: 10.1007/s10930-009-9166-3.
Using the data from Protein Data Bank the correlations of primary and secondary structures of proteins were analyzed. The correlation values of the amino acids and the eight secondary structure types were calculated, where the position of the amino acid and the position in sequence with the particular secondary structure differ at most 25. The diagrams describing these results indicate that correlations are significant at distances between -9 and 10. The results show that the substituents on Cbeta or Cgamma atoms of amino acid play major role in their preference for particular secondary structure at the same position in the sequence, while the polarity of amino acid has significant influence on alpha-helices and strands at some distance in the sequence. The diagrams corresponding to polar amino acids are noticeably asymmetric. The diagrams point out the exchangeability of residues in the proteins; the amino acids with similar diagrams have similar local folding requirements.
利用蛋白质数据库中的数据，对蛋白质的一级结构和二级结构的相关性进行了分析。计算了氨基酸与八种二级结构类型的相关值，其中氨基酸的位置与特定二级结构在序列中的位置差异最多为25。描述这些结果的图表表明，在-9至10的距离之间相关性显著。结果表明，氨基酸Cβ或Cγ原子上的取代基在序列中相同位置对特定二级结构的偏好中起主要作用，而氨基酸的极性在序列中一定距离处对α螺旋和β链有显著影响。对应极性氨基酸的图表明显不对称。这些图表指出了蛋白质中残基的可交换性；具有相似图表的氨基酸具有相似的局部折叠要求。
