Heitz F, Spach G, Trudelle Y
Biophys J. 1982 Oct;40(1):87-9. doi: 10.1016/S0006-3495(82)84462-7.
Analysis of the single-channel behavior of an analogue of gramicidin A in which all four tryptophyl residues are substituted by phenylalanyl suggests that the nature of the side chains may play an important role in the ion translocation process. Indeed, while infrared spectroscopy indicates that both peptides have very similar backbone conformations, they have different single-channel characteristics. The unit conductance of the analogue is much smaller than that of the natural product. Moreover, contrary to gramicidin A, it is voltage dependent.
对短杆菌肽A的类似物进行单通道行为分析，该类似物中所有四个色氨酸残基都被苯丙氨酸取代，结果表明侧链的性质可能在离子转运过程中起重要作用。实际上，虽然红外光谱表明两种肽具有非常相似的主链构象，但它们具有不同的单通道特征。该类似物的单位电导率远小于天然产物。此外，与短杆菌肽A相反，它是电压依赖性的。
