{'fraction_non_alphanumeric': 0.010392609699769052, 'fraction_numerical': 0.0011547344110854503, 'mean_word_length': 5.518796992481203, '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}}
Single molecule protein biophysics using chemically modified nanopores

The kinetics of protein folding and binding are not only scientifically relevant to understanding the complex molecular machine-like functionality of proteins inside of cells but can also help elucidate disease pathways and lead to better therapeutic agents. Using nanopores to investigate these kinetics holds great potential for such proteomic studies in which the structure and function of proteins can be rapidly screened. In this study, we achieve part of this goal by detecting the folded and unfolded states of BSA. Furthermore, we also show that protein sensing can be performed on more biologically significant protein domains such as PDZ2. To achieve this goal, pore fabrication methods and chemical surface modifications were investigated and optimized for efficient protein sensing.