Stoll R, Voelter W, Holak T A
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Institutes der Universität Tübingen, FRG.
Biopolymers. 1997 May;41(6):623-34. doi: 10.1002/(SICI)1097-0282(199705)41:6<623::AID-BIP3>3.0.CO;2-S.
The conformation of thymosin beta 9 in solution of 40% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol-d2 in water has been investigated by two-dimensional 1H-nmr spectroscopy. Under this condition thymosin beta 9 adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton distance constraints derived from nuclear Overhauser enhancement measurements. The conformation of thymosin beta 9 includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-terminus of thymosin beta 9 shows random-coil structure only.
通过二维¹H-核磁共振光谱研究了胸腺素β9在40%（v/v）1,1,1,3,3,3-六氟-2-丙醇-d2水溶液中的构象。在此条件下，胸腺素β9呈现出有序结构。该肽段构象的确定基于从核Overhauser效应测量中得出的一组304个近似质子间距离限制。胸腺素β9的构象包括从第4至27位残基以及第32至41位残基的两个螺旋区域。这两个螺旋被氨基酸28和31之间定义不明确的环区隔开；胸腺素β9的N端仅呈现无规卷曲结构。
