Chassaing G, Convert O, Lavielle S
Biochim Biophys Acta. 1986 Oct 17;873(3):397-404. doi: 10.1016/0167-4838(86)90089-0.
The three-dimensional structure of physalaemin, pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2, has been studied by one- and two-dimensional 500 MHz NMR spectroscopies in two solvents: methanol and dimethyl sulfoxide. As previously observed for substance P in methanol, the core of physalaemin 4----8 is folded into an helical conformation. This structure is stabilized by the presence of a salt bridge between Asp-3 and Lys-6 in both solvents. The only differences observed reside in the N-terminal sequences; the N-terminal tripeptide of substance is flexible whereas that of physalaemin is in an extended conformation.
在甲醇和二甲基亚砜两种溶剂中，运用一维及二维500兆赫核磁共振光谱法对雨蛙肽（pGlu-Ala-Asp-Pro-Asn-Lys-Phe-Tyr-Gly-Leu-Met-NH2）的三维结构进行了研究。正如之前在甲醇中观察到的P物质那样，雨蛙肽4至8的核心折叠成了螺旋构象。在两种溶剂中，Asp-3与Lys-6之间存在的盐桥使该结构得以稳定。观察到的唯一差异存在于N端序列；P物质的N端三肽具有柔性，而雨蛙肽的N端三肽则呈伸展构象。
