{'fraction_non_alphanumeric': 0.03469750889679715, 'fraction_numerical': 0.03202846975088968, 'mean_word_length': 5.859756097560975, '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}}
Design, synthesis, expression, and characterization of the genes for mouse FcγRIIb1 and FcγRIIb2 cytoplasmic regions

The cytoplasmic regions of the mouse low‐affinity FcγRII isoforms, mFcγRIIb1, and mFcγRIIb2, play a key role in signal transduction by mediating different cellular functions. mFcγRIIb1 has a 94‐residue cytoplasmic region, whereas mFcγRIIb2 has a 47‐residue cytoplasmic region. Genes encoding the cytoplasmic regions of mFcγRIIb1 (b1‐94) and mFcγRIIb2 (b2‐47) were designed, synthesized, and expressed as fusion proteins in Escherichia coli. A sequencespecific protease, thrombin, was used to release the b1‐94 peptide, which was purified by using HPLC. The b2‐47 peptide was synthesized chemically. CD spectropolarimetry was employed to examine the secondary structures of b1‐94 and b2‐47. These studies were conducted in aqueous solution, in mixtures of water and trifluoroethanol or methanol, and as a function of temperature. The results indicate that the b1‐94 and b2‐47 structures are sensitive functions of the solvent environment, and that nonaqueous solvents induce significant α‐helical structure.