NMR structure of human thymosin alpha-1.
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ABSTRACT:
SUBMITTER: Elizondo-Riojas MA
PROVIDER: S-EPMC3419376 | biostudies-literature | 2011 Dec
REPOSITORIES: biostudies-literature
Publications
NMR structure of human thymosin alpha-1.
Elizondo-Riojas Miguel-Angel MA Chamow Steven M SM Tuthill Cynthia W CW Gorenstein David G DG Volk David E DE
Biochemical and biophysical research communications 20111115 3-4
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 hel ...[more]
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