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Mazieres J, Paik PK, Garassino MC, Le X, Sakai H, Veillon R, et al
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
Eur J Cancer Oxf Engl
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