{'fraction_non_alphanumeric': 0.023485784919653894, 'fraction_numerical': 0.0, 'mean_word_length': 5.328125, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Nucleic acids-protein interactions: structural studies by x-ray diffraction and model building.

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.