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800MHz 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 beta-turns in the N-terminal twelve residues which form a distorted helical structure.
NMR structure of human thymosin alpha-1.,Elizondo-Riojas MA, Chamow SM, Tuthill CW, Gorenstein DG, Volk DE Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):356-61. Epub 2011 Nov 15. PMID:22115779[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Elizondo-Riojas MA, Chamow SM, Tuthill CW, Gorenstein DG, Volk DE. NMR structure of human thymosin alpha-1. Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):356-61. Epub 2011 Nov 15. PMID:22115779 doi:10.1016/j.bbrc.2011.11.041
