Fidelio G D, Austen B M, Chapman D, Lucy J A
Biochem J. 1986 Aug 15;238(1):301-4. doi: 10.1042/bj2380301.
The surface behaviour of three signal-sequence polypeptides (the pretrypsinogen 2 signal sequence, a synthetic consensus signal sequence and the putative signal sequence of ovalbumin) were studied at an air-water interface. It was found that the surface stabilities of the spread polypeptide films were higher than those of polypeptides and proteins previously investigated (including melittin and membrane proteins), and that the signal peptides had a much lower affinity for the interface than had other peptides and proteins. The observed molecular areas of the signal-sequence peptides indicated that the molecules have a considerable degree of secondary structure at the surface interface.
研究了三种信号序列多肽（胰蛋白酶原2前体信号序列、合成共有信号序列和卵清蛋白假定信号序列）在气-水界面的表面行为。结果发现，铺展的多肽膜的表面稳定性高于先前研究的多肽和蛋白质（包括蜂毒肽和膜蛋白），并且信号肽对界面的亲和力远低于其他肽和蛋白质。信号序列肽的观察分子面积表明，这些分子在表面界面具有相当程度的二级结构。
