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[DOI] [PMC free article] [PubMed] [Google Scholar] [167].Ghouri YA, Richards DM, Rahimi EF, Krill JT, Jelinek KA, DuPont AW

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