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2023;379(6633):eade7114
doi:10.1111/ger.12044 4
NMR spectroscopy studies confirm that Thymosin 4 behaves as an intrinsically disordered protein with preferential -helical conformations at residues 5-16 and 31-37 under specific conditions (pH 3.0-6.5, temperature 1-14C), though the fragment region maintains less defined secondary structure
