人胸腺肽 α-1 的 NMR 结构。
NMR structure of human thymosin alpha-1.
机构信息
Center for Proteomics and Systems Biology, Institute of Molecular Medicine for Prevention of Human Diseases, Department of NanoMedicine and Biomedical Engineering, University of Texas Health Science Center-Houston, 1825 Pressler, Houston, TX 77030, United States.
出版信息
Biochem Biophys Res Commun. 2011 Dec 16;416(3-4):356-61. doi: 10.1016/j.bbrc.2011.11.041. Epub 2011 Nov 15.
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.
摘要
已确定 28 残基肽胸腺肽 α-1 在 40%TFE/60%水（v/v）中的 800 MHz NMR 结构。使用含有 40%TFE/60%TIP3P 水（v/v）的显式溶剂盒进行约束分子动力学模拟，以获得 NMR 结构的 3D 模型。我们发现该肽采用具有两个稳定区域的结构化构象：从残基 14 到 26 的α-螺旋区域和 N-末端十二个残基中的两个双β-转角，形成扭曲的螺旋结构。
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