NMR structure of human thymosin alpha-1

作者：Elizondo Riojas Miguel Angel; Chamow Steven M; Tuthill Cynthia W; Gorenstein David G; Volk David E^*

来源：Biochemical and Biophysical Research Communications, 2011, 416(3-4): 356-361.

DOI：10.1016/j.bbrc.2011.11.041

• NMR data collection
• Chemical shift assignment
• Protein structure determination
• Thymosin alpha1
• Thymalfasin
• Trifluroethanol

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 beta-turns in the N-terminal twelve residues which form a distorted helical structure.

• 出版日期2011-12-16