{'fraction_non_alphanumeric': 0.020273248126928163, 'fraction_numerical': 0.002644336712208021, 'mean_word_length': 5.676470588235294, '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}}
Molecular recognition of intrinsically disordered proteins: theory, predictions and applications

In the last decade of the 20 th century the results of high-throughput genomic studies drastically changed our view of structures and biological roles of proteins. Until the early 1990's the basic assumption of structural biology was that the structure of a protein is indispensable to its proper function. However, the accumulation of known proteins contradicting this 'structure-function paradigm' forced molecular biologists to reassess this prevailing view. These intrinsically disordered/unstructured proteins (IDPs/IUPs) do not have a stable, three dimensional structure in isolation, even under physiological conditions, yet they are able to perform highly specific and crucial functions in signaling, transcription and various regulatory processes, such as the control of cell division and apoptosis. Given the functional importance of IUPs, many proteins containing disordered regions have been associated with various diseases such as diabetes, amyloidosis, neurodegenerative diseases and cancer. These results lead to the conclusion that protein disorder comes with a 'biological cost' that is reflected in an increased risk of cancer and other diseases. Although lacking a stable structure in isolation, IDPs can adopt a well-defined conformation upon specific interactions with partner molecules, most often other proteins or RNA/DNA. This coupled-folding-and-binding process distinguishes the binding of disordered proteins from that of globular proteins. The loss of large degrees of freedom of the disordered partner during the binding uncouples specificity from the binding strength. This way IDPs are more prone to form specific, yet transient interactions, which are indispensable to regulatory and signaling processes. The unique features of the binding of disordered proteins enable them to mediate a large number of interactions thus serving as hubs of protein-protein interaction networks. Parallel to the disordered binding region concept, interaction between short regions of proteins and globular domains has been extensively studied using the concept of linear motifs. In this framework, the description of the molecular recognition is based on