Wimley W C, White S H
Department of Physiology and Biophysics, University of California, Irvine 92697-4560, USA.
Nat Struct Biol. 1996 Oct;3(10):842-8. doi: 10.1038/nsb1096-842.
The partitioning of membrane-active oligopeptides into membrane interfaces promotes the formation of secondary structure. A quantitative description of the coupling of structure formation to partitioning, which may provide a basis for understanding membrane protein folding and insertion, requires an appropriate free energy scale for partitioning. A complete interfacial hydrophobicity scale that includes the contribution of the peptide bond was therefore determined from the partitioning of two series of small model peptides into the interfaces of neutral (zwitterionic) phospholipid membranes. Aromatic residues are found to be especially favoured at the interface while charged residues, and the peptide bond, are disfavoured about equally. Reduction of the high cost of partitioning the peptide bond through hydrogen bonding may be important in the promotion of structure formation in the membrane interface.
具有膜活性的寡肽在膜界面的分配促进了二级结构的形成。对结构形成与分配之间耦合的定量描述，可为理解膜蛋白折叠和插入提供基础，这需要一个合适的分配自由能标度。因此，通过将两系列小模型肽分配到中性（两性离子）磷脂膜界面，确定了一个完整的界面疏水性标度，其中包括肽键的贡献。发现芳香族残基在界面处特别有利，而带电荷残基和肽键则同样不利。通过氢键降低肽键分配的高成本，可能对促进膜界面的结构形成很重要。
