title: NMR structure of human thymosin alpha-1.
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.
authors: Center for Proteomics and Systems Biology, Institute of Molecular Medicine for Prevention of Human Diseases, Department of NanoMedicine and Biomedical Engineering, University of Texas Health Science Center-Houston, 1825 Pressler, Houston, TX 77030, United States.
authors: Miguel-Angel
authors: MA
authors: Elizondo-Riojas
authors: Steven M
authors: SM
authors: Chamow
authors: Cynthia W
authors: CW
authors: Tuthill
authors: David G
authors: DG
authors: Gorenstein
authors: David E
authors: DE
authors: Volk
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D000077596:Thymalfasin; D013947:Thymosin / Q000031:analogs & derivatives* / Q000737:chemistry
chemical_list: D013947:Thymosin; D000077596:Thymalfasin