Williamson M P, Hall M J, Handa B K
Eur J Biochem. 1986 Aug 1;158(3):527-36. doi: 10.1111/j.1432-1033.1986.tb09786.x.
The peptide alpha Ahx-Met-Ala-Asp-Pro-Asn-Arg-Phe-Arg-Gly-Lys-Asp-Leu-Pro-Val-Leu- Asp-Gln-Leu-Thr-Asp-Pro-Pro-alpha Ahx (epsilon Ahx = 6-aminohexanoyl), the antigenic sequence 11-32 from Herpes simplex virus glycoprotein D-1, has been synthesised. Its 1H-NMR spectrum has been assigned by a combination of two-dimensional techniques in H2O and 2H2O. Its secondary structure has been defined by nuclear Overhauser effects and amide proton exchange rates, and also to some extent chemical shifts, coupling constants and amide proton temperature coefficients. These latter parameters are shown to be less reliable as guides to secondary structure. The peptide has a helical (type I/III) turn at residues Pro-14-Asn-15 and helical structure at residues Lys-20-Val-24, in rapid equilibrium with random-coil structure. A beta-turn at residues Arg-18-Gly-19 may be present as a minor component. These locations of secondary structure correspond with previously determined regions of antigenic activity.
已合成肽α Ahx - Met - Ala - Asp - Pro - Asn - Arg - Phe - Arg - Gly - Lys - Asp - Leu - Pro - Val - Leu - Asp - Gln - Leu - Thr - Asp - Pro - Pro -α Ahx（ε Ahx = 6 - 氨基己酰基），其为来自单纯疱疹病毒糖蛋白D - 1的抗原序列11 - 32。通过在H₂O和²H₂O中二维技术的组合确定了其¹H - NMR谱。通过核Overhauser效应和酰胺质子交换速率，并在一定程度上通过化学位移、耦合常数和酰胺质子温度系数确定了其二级结构。结果表明，后述参数作为二级结构的指导不太可靠。该肽在残基Pro - 14 - Asn - 15处有一个螺旋（I/III型）转角，在残基Lys - 20 - Val - 24处有螺旋结构，与无规卷曲结构处于快速平衡。在残基Arg - 18 - Gly - 19处可能存在一个β转角作为次要成分。这些二级结构位置与先前确定的抗原活性区域相对应。
