Jacchieri S G
Fundação Antônio Prudente, São Paulo, Brazil.
Mol Divers. 1998;4(3):199-207. doi: 10.1023/a:1009683618729.
Six computer-based combinatorial libraries, including tetrapeptide sequences (generated with five amino acids) and conformations (generated with five main chain and three side chain rotamers), were obtained and sequence-conformation probabilities were calculated with a molecular and statistical mechanics procedure. The structural motifs alpha-helix, beta-sheet, 3(10)-helix, reverse turn I and gamma-turn were focused in these calculations. It is shown that sequence-conformation-probability surfaces provide a broad view of structural changes accompanying changes in sequence. Numerical indices are defined to enable comparisons between frequencies of occurrence of these structural motifs in peptide libraries and in a database of low sequence identity protein structures. Fine details of sequence-conformation-probability surfaces show the effect of point mutations. Broad comparisons between different regions of these surfaces indicate how to select the occurrence of structural motifs in the combinatorial synthesis of peptide chains.
获得了六个基于计算机的组合文库，包括四肽序列（由五种氨基酸生成）和构象（由五个主链和三个侧链旋转异构体生成），并使用分子和统计力学程序计算了序列 - 构象概率。这些计算聚焦于α - 螺旋、β - 折叠、3(10) - 螺旋、反向转角I和γ - 转角等结构基序。结果表明，序列 - 构象概率表面提供了伴随序列变化的结构变化的广泛视图。定义了数值指标，以便能够比较这些结构基序在肽文库和低序列同一性蛋白质结构数据库中的出现频率。序列 - 构象概率表面的精细细节显示了点突变的影响。这些表面不同区域之间的广泛比较表明了如何在肽链的组合合成中选择结构基序的出现。
