Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 416, Issue 3-4, Pages 356-361Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2011.11.041
Keywords
NMR data collection; Chemical shift assignment; Protein structure determination; Thymosin alpha1; Thymalfasin; Trifluroethanol
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Funding
- SciClone Pharmaceutical
- W.M. Keck Foundation
- John S. Dunn, Sr. Foundation
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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. (C) 2011 Elsevier Inc. All rights reserved,
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