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• W2075429965 abstract "800 MHz NMR structure of the 28-residue peptide thymosin alpha-1 in 40% TFE/60% water (v/v) has been determined. Restrained molecular dynamic simulations with an explicit solvent box containing 40% TFE/60% TIP3P water (v/v) were used, in order to get the 3D model of the NMR structure. We found that the peptide adopts a structured conformation having two stable regions: an alpha-helix region from residues 14 to 26 and two double β-turns in the N-terminal twelve residues which form a distorted helical structure." @default.
• W2075429965 created "2016-06-24" @default.
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• W2075429965 date "2011-12-01" @default.
• W2075429965 modified "2023-10-17" @default.
• W2075429965 title "NMR structure of human thymosin alpha-1" @default.
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• W2075429965 doi "https://doi.org/10.1016/j.bbrc.2011.11.041" @default.
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