Yang J T, Bewley T A, Chen G C, Li C H
Proc Natl Acad Sci U S A. 1977 Aug;74(8):3235-8. doi: 10.1073/pnas.74.8.3235.
Circular dichroic spectra of camel beta-endorphin and ovine beta-lipotropin in water show little, if any, secondary structure. Intrinsic viscosities and sedimentation coefficients of the two peptides also suggest that the molecules are not compact and globular. Methanol or sodium dodecyl sulfate promotes the formation of helical structure to an extent as much as one-half of either peptide molecule. The conformation of the complex between camel beta-endorphin and dodecyl sulfate may be related to the opiate-like function of this peptide hormone.
骆驼β-内啡肽和绵羊β-促脂解素在水中的圆二色光谱显示几乎没有二级结构(即便有也极少)。这两种肽的特性粘度和沉降系数也表明其分子并非紧密的球状结构。甲醇或十二烷基硫酸钠可促进螺旋结构的形成,其程度高达任一肽分子的一半。骆驼β-内啡肽与十二烷基硫酸钠之间复合物的构象可能与其作为肽类激素的阿片样功能有关。