{'fraction_non_alphanumeric': 0.03278688524590164, 'fraction_numerical': 0.012610340479192938, 'mean_word_length': 5.352, '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}}
Conformation of four peptides corresponding to the α‐helical segments of human GM–CSF

The conformation of segments corresponding to the four α‐helical stretches found in human granulocyte‐macrophage colony‐stimulating factor was studied in water solution in the presence of different amounts of 2,2,2‐trifluoroethanol (TFE). The CD spectra reveal the onset of secondary structure upon addition of TFE. The final amount of helical conformation varies among the four peptides. In all cases, the conformational transition is complete before 50% TFE (v/v). 1H‐NMR studies were conducted at this solvent composition, leading to the assignment of all the resonances and to the definition of the secondary structure for all four fragments. © 1997 European Peptide Society and John Wiley & Sons, Ltd.