NMR structure of human thymosin alpha-1
| Autor: | David G. Gorenstein, Cynthia W. Tuthill, Steven M. Chamow, David E. Volk, Miguel-Angel Elizondo-Riojas |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Thymalfasin Molecular Sequence Data Biophysics Thymosin Peptide 3d model Cell Biology Biochemistry Protein Structure Secondary Article Solvent Crystallography Molecular dynamics chemistry Thymosin alpha Humans Amino Acid Sequence Nuclear Magnetic Resonance Biomolecular Molecular Biology Peptide sequence |
| Zdroj: | Biochemical and Biophysical Research Communications. 416:356-361 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2011.11.041 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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