NMR structure of human thymosin alpha-1.

Biochemical and biophysical research communications2011PMID: 22115779

View on PubMed DOI: 10.1016/j.bbrc.2011.11.041

Plain Language Summary

Scientists determined the three-dimensional structure of thymosin alpha-1 using high-resolution NMR spectroscopy. The 28-residue peptide was found to have two distinct structural regions: an alpha-helix spanning residues 14 to 26 and a pair of double beta-turns at the N-terminal end forming a distorted helical shape.

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

Elizondo-Riojas, Miguel-Angel; Chamow, Steven M; Tuthill, Cynthia W; Gorenstein, David G; Volk, David E