Kim S H
Prog Clin Biol Res. 1980;40:311-7.
X-ray diffraction and model-building studies suggest that the alpha-helix and beta-structure of protein may interact with double-helix nucleic acids. In the former case basic side chains of amino acid residues in the alpha-helix can interact with phosphate groups of the double helix, and in the latter case the peptide backbone in a beta-ribbon can hydrogen-bond to the backbone of the double helix of nucleic acids. These structurally compatible interactions between well-known secondary structures of protein and the double helix provide models for understanding specific interaction between nucleic acid and protein during general recognition, or preliminary stages before base sequence-specific recognition.
X射线衍射和模型构建研究表明，蛋白质的α螺旋和β结构可能与双螺旋核酸相互作用。在前一种情况下，α螺旋中氨基酸残基的碱性侧链可与双螺旋的磷酸基团相互作用；在后一种情况下，β折叠中的肽主链可与核酸双螺旋的主链形成氢键。蛋白质的这些已知二级结构与双螺旋之间在结构上的兼容相互作用，为理解核酸与蛋白质在一般识别过程中，或在碱基序列特异性识别之前的初始阶段的特异性相互作用提供了模型。
