{'fraction_non_alphanumeric': 0.029012345679012345, 'fraction_numerical': 0.0049382716049382715, 'mean_word_length': 5.698347107438017, '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}}
Circular dichroism studies on conformational changes in protein molecules upon adsorption on ultrafine polystyrene particles

The conformational changes in well‐characterized model proteins [bovine ribonuclease A (RNase A), horseradish peroxidase, sperm‐whole myoglobin, human hemoglobin, and bovine serum albumin (BSA)] upon adsorption on ultrafine polystyrene (PS) particles have been studied using circular dichroism (CD) spectroscopy. These proteins were chosen with special attention to molecular flexibility. The ultrafine PS particles were negatively charged and have average diameters of 20 or 30 nm. Utilization of these ultrafine PS particles makes it possible to apply the CD technique to determine the secondary structure of proteins adsorbed on the PS surface. Effects of protein properties and adsorption conditions on the extent of the changes in the secondary structure of protein molecules upon adsorption on ultrafine PS particles were studied. The CD spectrum changes upon adsorption were significant in the “soft” protein molecules (myoglobin, hemoglobin, and BSA), while they were insingnificant in the “rigid” proteins (RNase A and peroxidase). The soft proteins sustained a marked decrease in α‐helix content upon adsorption. Moreover, the native α‐helix content, which is given as the percentage of the α‐helix content in the free proteins, of adsorbed BSA was found to decrease with decreasing pH and increase with increasing adsorbed amount. These observations confirm some well‐known hypotheses for the confirmational chages in protein molecules upon adsorption. © 1992 John Wiley & Sons, Inc.